Crystal structure of hen egg-white lysozyme at a hydrostatic pressure of 1000 atmospheres

Kundrot, Craig E.; Richards, Frederic M.

doi:10.1016/0022-2836(87)90634-6

Cited by 338 publications

(269 citation statements)

References 34 publications

Supporting

Mentioning

238

Contrasting

Order By: Relevance

“…~ 1995 International Union of Crystallography Printed in Great Britain -all rights reserved resolution X-ray data (Rao, Hogle & Sundaralingam, 1983;Berthou, Lifchitz, Artymiuk & Jollts, 1983;Kundrot & Richards, 1987;Ramanadham, Sieker & Jensen, 1990). In the crystalline state, lysozyme binds Nacetylglucosamine (NAG) and its oligomers (Johnson et al, 1988).…”

Section: Introductionmentioning

confidence: 99%

X-ray structure of turkey egg lysozyme complex with di-N-acetyl-chitobiose. Recognition and binding of α-anomeric form

Harata¹,

Muraki²

1995

Acta Cryst D

View full text Add to dashboard Cite

The crystalline complex of turkey-egg lysozyme (TEL) with di-N-acetylchitobiose (NAG2) was prepared by a soaking method and the structure was determined by Xray analysis at 1.55/~, resolution. The structure was refined to an R value of 0.175 by simulated annealing and energy minimization. The a-anomer of NAG2 is located at subsite D with the orientation perpendicular to the direction of the active-site cleft. The anomeric residue is deeply inserted into the cleft and the O1 --H hydroxyl group is hydrogen bonded to the carboxyl group of Glu35 which is a catalytic residue. The other sugar residue protrudes outside the cleft and is in van der Waals contact with the E-sheet region comprising of residues 43-53. The binding of NAG2 makes the activesite cleft 0.3-0.5 ,~ narrower and supresses the thermal motion of two lobes constructing the cleft. The NAG2 molecule is bound in a manner not assumed in the catalytic action of the enzyme and the geometry of binding indicates that the a-anomer blocks the active center and acts only as an inhibitor.

show abstract

Section: Introductionmentioning

confidence: 99%

X-ray structure of turkey egg lysozyme complex with di-N-acetyl-chitobiose. Recognition and binding of α-anomeric form

Harata¹,

Muraki²

1995

Acta Cryst D

View full text Add to dashboard Cite

show abstract

“…Pressure studies on BPTI include the pressure dependence of H N and H a chemical shifts~Li et al, 1998! and of aromatic ring flip rates~Wagner, 1980!, and high pressure molecular dynamics simulations~Kitchen et al, 1992;Brunne & van Gunsteren, 1993;Wroblowski et al, 1996!. Other important methods used to monitor the behavior of proteins as a function of pressure include ultrasonic compressibilitỹ Gekko & Noguchi, 1979;Gekko & Hasegawa, 1986;Zollfrank et al, 1991a;Kharakoz & Sarvazyan, 1993;Kharakoz, 1997!, optical absorption~Hawley, 1971Zipp & Kauzmann, 1973!, enzymatic activity~Taniguchi & Suzuki, 1983!, fluorescence~Pala-dini & Weber, 1981Cioni & Strambini, 1996!, infrared~Takeda et al, 1995!, stress field~Kobayashi et al, 1997!, hole-burning Zollfrank et al, 1991bHuang et al, 1997!, small angle X-ray scattering~Panick et al, 1998!, and crystallographic experiments Kundrot & Richards, 1987!. Useful reviews on pressure effects on proteins are also available~Gross & Jaenicke, 1994; Jonas & Jonas, 1994;Heremans & Smeller, 1998!.…”

mentioning

confidence: 99%

Pressure response of protein backbone structure. Pressure‐induced amide ¹⁵N chemical shifts in BPTI

et al. 1999

View full text Add to dashboard Cite

The effect of pressure on amide 15 N chemical shifts was studied in uniformly 15 N-labeled basic pancreatic trypsin inhibitor~BPTI! in 90% 1 H 2 O010% 2 H 2 O, pH 4.6, by 1 H-15 N heteronuclear correlation spectroscopy between 1 and 2,000 bar. Most 15 N signals were low field shifted linearly and reversibly with pressure~0.468 6 0.285 ppm02 kbar!, indicating that the entire polypeptide backbone structure is sensitive to pressure. A significant variation of shifts among different amide groups~0-1.5 ppm02 kbar! indicates a heterogeneous response throughout within the three-dimensional structure of the protein. A tendency toward low field shifts is correlated with a decrease in hydrogen bond distance on the order of 0.03 Å02 kbar for the bond between the amide nitrogen atom and the oxygen atom of either carbonyl or water. The variation of 15 N shifts is considered to reflect site-specific changes in f, c angles. For b-sheet residues, a decrease in c angles by 1-2802 kbar is estimated. On average, shifts are larger for helical and loop regions~0.553 6 0.343 and 0.519 6 0.261 ppm02 kbar, respectively! than for b-sheet~0.295 6 0.195 ppm02 kbar!, suggesting that the pressure-induced structural changes~local compressibilities! are larger in helical and loop regions than in b-sheet. Because compressibility is correlated with volume fluctuation, the result is taken to indicate that the volume fluctuation is larger in helical and loop regions than in b-sheet. An important aspect of the volume fluctuation inferred from pressure shifts is that they include motions in slower time ranges~less than milliseconds! in which many biological processes may take place.

show abstract

“…Molecular volumes determined from solution measurements are by roughly 10% larger than those calculated by Kundrot and Richards from the crystal structure [3]. If this difference represented real physical changes rather than the sum of the systematic errors of both methods, crystallization ought to be strongly …”

Section: Discussionmentioning

confidence: 82%

“…A lO!tl aliquot was diIuted 60-fold in water, centrifuged and subjected to photometric concentration measurement at 280 nm. The ~~~~~~~ I~,,, was taken to be 2.56, 3. RESULTS First attempts to crystallize lysozyme at high hydrostatic pressure yieIded a reduced number of crystals compared to the normal pressure reference, but both kinds of crystals grew to the same size within the same incubation time, This was taken as a hint to an inhibition of nucleation by pressure.…”

Section: * This Paper Is Dedicated To Tabitha Nnomi Grofl Born 29 Mamentioning

confidence: 99%

“…on the rate of growth or final quality of protein crystals' [ 11. Previous papers dealing with both pressure and protein crystallization were limited either to large-scale growth of small crystals for technical purposes [2], or to high pressure X-ray analysis of crystals grown at atmospheric pressure [3,4]. The obvious pendant to the latter studies, namely the analysis of pressure grown crystals at ambient and at growth pressure has not yet been undertaken.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Growth inhibition of lysozyme crystals at high hydrostatic pressure

Groß

Jaenicke

1991

FEBS Letters

View full text Add to dashboard Cite

The influence of high hydiostatic pressures on the crystallization of hen egpwhite lysozyme has been determined by growing lysozyme crystals with a capillary technique adapted to high pressure conditions and monitoring the residual protein concentration remaining in the supematant.Pressure is found to reduce the rate of crystallization and to enhance the solubility of lysozymc in 1 M NaCl. pH 4.66. The volume change calculated from the latter result amounts to 12.5 ml/moI. This value is too small to be detectable by comparison of total molar volumes.

show abstract

Crystal structure of hen egg-white lysozyme at a hydrostatic pressure of 1000 atmospheres

Cited by 338 publications

References 34 publications

X-ray structure of turkey egg lysozyme complex with di-N-acetyl-chitobiose. Recognition and binding of α-anomeric form

X-ray structure of turkey egg lysozyme complex with di-N-acetyl-chitobiose. Recognition and binding of α-anomeric form

Pressure response of protein backbone structure. Pressure‐induced amide ¹⁵N chemical shifts in BPTI

Growth inhibition of lysozyme crystals at high hydrostatic pressure

Contact Info

Product

Resources

About

Crystal structure of hen egg-white lysozyme at a hydrostatic pressure of 1000 atmospheres

Cited by 338 publications

References 34 publications

X-ray structure of turkey egg lysozyme complex with di-N-acetyl-chitobiose. Recognition and binding of α-anomeric form

X-ray structure of turkey egg lysozyme complex with di-N-acetyl-chitobiose. Recognition and binding of α-anomeric form

Pressure response of protein backbone structure. Pressure‐induced amide 15N chemical shifts in BPTI

Growth inhibition of lysozyme crystals at high hydrostatic pressure

Contact Info

Product

Resources

About

Pressure response of protein backbone structure. Pressure‐induced amide ¹⁵N chemical shifts in BPTI