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1F74

CRYSTAL STRUCTURE ANALYSIS OF N-ACETYLNEURAMINATE LYASE FROM HAEMOPHILUS INFLUENZAE: CRYSTAL FORM II COMPLEXED WITH 4-DEOXY-SIALIC ACID

Summary for 1F74
Entry DOI10.2210/pdb1f74/pdb
Related1F5Z 1F6K 1F6P 1F73 1F7B 1FDY 1FDZ 1NAL
DescriptorN-ACETYL-NEURAMINATE LYASE, 6,7,8,9-TETRAHYDROXY-5-METHYLCARBOXAMIDO-2-OXONONANOIC ACID, GLYCEROL, ... (5 entities in total)
Functional Keywordsbeta barrel, lyase
Biological sourceHaemophilus influenzae
Cellular locationCytoplasm: P44539
Total number of polymer chains2
Total formula weight66113.51
Authors
Barbosa, J.A.R.G.,Smith, B.J.,DeGori, R.,Lawrence, M.C. (deposition date: 2000-06-26, release date: 2000-11-22, Last modification date: 2024-02-07)
Primary citationBarbosa, J.A.R.G.,Smith, B.J.,DeGori, R.,Ooi, H.C.,Marcuccio, S.M.,Campi, E.M.,Jackson, W.R.,Brossmer, R.,Sommer, M.,Lawrence, M.C.
Active site modulation in the N-acetylneuraminate lyase sub-family as revealed by the structure of the inhibitor-complexed Haemophilus influenzae enzyme.
J.Mol.Biol., 303:405-421, 2000
Cited by
PubMed Abstract: The N-acetylneuraminate lyase (NAL) sub-family of (beta/alpha)(8) enzymes share a common catalytic step but catalyse reactions in different biological pathways. Known examples include NAL, dihydrodipicolinate synthetase (DHDPS), d-5-keto-4-deoxyglucarate dehydratase, 2-keto-3-deoxygluconate aldolase, trans-o-hydroxybenzylidenepyruvate hydrolase-aldolase and trans-2'-carboxybenzalpyruvate hydratase-aldolase. Little is known about the way in which the three-dimensional structure of the respective active sites are modulated across the sub-family to achieve cognate substrate recognition. We present here the structure of Haemophilus influenzae NAL determined by X-ray crystallography to a maximum resolution of 1.60 A, in native form and in complex with three substrate analogues (sialic acid alditol, 4-deoxy-sialic acid and 4-oxo-sialic acid). These structures reveal for the first time the mode of binding of the complete substrate in the NAL active site. On the basis of the above structures, that of substrate-complexed DHDPS and sequence comparison across the sub-family we are able to propose a unified model for active site modulation. The model is one of economy, allowing wherever appropriate the retention or relocation of residues associated with binding common substrate substituent groups. Our structures also suggest a role for the strictly conserved tyrosine residue found in all active sites of the sub-family, namely that it mediates proton abstraction by the alpha-keto acid carboxylate in a substrate-assisted catalytic reaction pathway.
PubMed: 11031117
DOI: 10.1006/jmbi.2000.4138
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.6 Å)
Structure validation

229380

數據於2024-12-25公開中

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