Alignment of Beta-barrels in (β/α)8 Proteins using Hydrogen-bonding Pattern

Sergeev, Yu. V.; Lee, B.

doi:10.1006/jmbi.1994.1717

Cited by 24 publications

(17 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…This could indicate that b-sheet regions in the xylanase protein are well conserved across long evolutionary times, whereas a-helix regions are relatively less conserved. This would be in agreement with the observation that the b-barrel is the most highly conserved structural feature across TIM-barrel families (Pickett et al, 1992;Sergeev & Lee, 1994).…”

Section: Effects Of Adding Homologous Sequencessupporting

confidence: 87%

Using Evolutionary Trees in Protein Secondary Structure Prediction and Other Comparative Sequence Analyses

Goldman

Thorne²,

Jones³

1996

Journal of Molecular Biology

107

View full text Add to dashboard Cite

Section: Effects Of Adding Homologous Sequencessupporting

confidence: 87%

Using Evolutionary Trees in Protein Secondary Structure Prediction and Other Comparative Sequence Analyses

Goldman

Thorne²,

Jones³

1996

Journal of Molecular Biology

107

View full text Add to dashboard Cite

“…Further, it has been speculated, from a study of several a/fl-barrel enzymes, that circular permutations may already have occurred [43]. It is exciting, therefore, that natu- Fig.…”

Section: Sequence Alignment and (Ilia)s-barrel Elements Inmentioning

confidence: 99%

A circularly permuted α‐amylase‐type α/β‐barrel structure in glucan‐synthesizing glucosyltransferases

1996

View full text Add to dashboard Cite

A motif of amino acid residues, located at the active site and specific j~-strands in a-amylases, is recognized in a-l,3-and a-l,6-glucan-synthesizing glucosyltransferases, leading to the conclusion that these enzymes contain an aliB-barrel closely related to the (~la)s-fold of the a-amylase superfamily. The secondary structure elements of the transferase barrel, however, are circularly permuted to start with an a-helix equivalent to helix 3 in the a-amylases. Thus, the transferase counterpart of the long third ~ -+ a connection -constituting a domain in the c~-amylases -is divided to precede and succeed the barrel. This architectural arrangement may be coupled to sucrose scission and glucosyl transfer. The involvement in the mechanism in glucosyitransferases of active site residues recurring in amylolytic enzymes is discussed.

show abstract

“…They have also been described either in specific cases, as for ( f i / 0 1 )~ barrel proteins (Sergeev & Lee, 1994), or in more general database searches (Alexandrov & Go, 1994).…”

Section: Resultsmentioning

confidence: 99%

The structural homology between uteroglobin and the pore‐forming domain of colicin A suggests a possible mechanism of action for uteroglobin

Cruz

Lee

1996

Protein Science

Self Cite

View full text Add to dashboard Cite

Although the exact physiological function of uteroglobin is not known, it has been suggested that it may function by inhibiting phospholipase Az. We have found that the uteroglobin fold is embedded in that of the poreforming domain of colicin A. Colicin A is an antibiotic protein that kills sensitive Escherichia coli cells by forming a pore in their phospholipid membrane. The RMS deviation between the C, atoms after the structural alignment is 2.39 A for the 52 superimposed residues. In the alignment, uteroglobin helices 1, 2, 3, and 4 align with colicin A helices 6, 7, 3, and 4, respectively. The motif is strongly amphipathic in both proteins. On the basis of this common structural motif and of known experimental data on both proteins, we propose that UG binds to the membrane surface by lying on it monotopically. The phospholipase A2 inhibition would follow this initial binding step.

show abstract

Alignment of Beta-barrels in (β/α)8 Proteins using Hydrogen-bonding Pattern

Cited by 24 publications

References 0 publications

Using Evolutionary Trees in Protein Secondary Structure Prediction and Other Comparative Sequence Analyses

Using Evolutionary Trees in Protein Secondary Structure Prediction and Other Comparative Sequence Analyses

A circularly permuted α‐amylase‐type α/β‐barrel structure in glucan‐synthesizing glucosyltransferases

The structural homology between uteroglobin and the pore‐forming domain of colicin A suggests a possible mechanism of action for uteroglobin

Contact Info

Product

Resources

About