The stereochemistry at carbon 3 of pyruvate lyase condensation products. 2-Keto-3-deoxygluconate-6-phosphate aldolase.

Meloche, H. Paul; Mehler, Louise; Wurster, J M

doi:10.1016/s0021-9258(19)41012-0

Cited by 9 publications

(1 citation statement)

References 18 publications

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“…KDPG aldolase is one of the more thoroughly studied aldolases, structurally (Hammerstedt et al, 1971;Robertson et al, 1971 a,b;Barran and Wood, 1971;Mohler et al, 1972;Vandlen et al, 1973) and mechanistically (Grazi et al, 1963;Ingram and Wood, 1966;Rose and O'Connell, 1967;Meloche, 1970;Meloche and Glusker, 1973;Meloche et al, 1975). As a result, it has become a model of aldolytic catalysis comparable to that of FDP aldolase.…”

mentioning

confidence: 99%

The folding and quaternary structure of trimeric 2-keto-3-deoxy-6-phosphogluconic aldolase at 3.5- Å resolution

Mavridis¹,

Tulinsky²

1976

Biochemistry

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An X-ray crystallographic structure determination has been carried out on 2-keto-3-deoxy-6-phosphogluconic (KDPG) aldolase at 3.5-A resolution using the multiple isomorphous replacement method with three heavy atom derivatives along with anomalous dispersion contributions from two of the derivatives. Crystals grown from ammonium sulfate-phosphate buffered (pH 3.5) solutions were: cubic, a= 103.40 (4) A, space group P213. KDPG aldolase consists of trimeric heterologous assemblages utilizing crystallographic threefold symmetry. The overall profile of the oligomeric structure viewed down the threefold axis resembles that of a ship propeller while the subunits are approximate irregular oblate ellipsoids (25 X 45 X 45 A). The folding of most of the polypeptide chain was traced unambiguously. Secondary structural features consist of nine helical regions (75 residues, 35%) and a pair of two parallel chains. The subunit contains a long empty channel which is about 9 X 9 X 30 A with one of the pair of parallel chains forming part of the wall. Three mercury binding sites are located in this channel. These might correspond to the two readily accessible and one of the two buried cysteine residues of each subunit. The channel terminates with another cavity of about 8 X 10 X 25 A near the surface of the oligomeric structure. The regions of the subunits near the threefold axis are characterized by a high degree of secondary structural organization and these make close intersubunit contacts. Quarternary interactions are due mainly to side-chain interactions of helices.

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