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PDBsum entry 2wpb
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Contents |
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* Residue conservation analysis
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PDB id:
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Lyase
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Title:
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Crystal structure of the e192n mutant of e. Coli n-acetylneuraminic acid lyase in complex with pyruvate and the inhibitor (2r,3r)-2,3,4- trihydroxy-n,n-dipropylbutanamide in space group p21 crystal form i
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Structure:
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N-acetylneuraminate lyase. Chain: a, b, c, d. Fragment: residues 2-297. Synonym: n-acetyl-neuraminic acid lyase, n-acetylneuraminic acid aldolase, n-acetylneuraminate pyruvate-lyase, sialic acid lyase, sialate lyase, sialic acid aldolase, nalase. Engineered: yes. Mutation: yes. Other_details: schiff base between lys165 and pyruvate in all chains
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Source:
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Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 469008.
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Resolution:
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2.05Å
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R-factor:
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0.192
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R-free:
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0.234
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Authors:
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I.Campeotto,A.H.Bolt,T.A.Harman,C.H.Trinh,C.A.Dennis,S.E.V.Phillips, A.R.Pearson,A.Nelson,A.Berry
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Key ref:
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I.Campeotto
et al.
(2010).
Structural insights into substrate specificity in variants of N-acetylneuraminic Acid lyase produced by directed evolution.
J Mol Biol,
404,
56-69.
PubMed id:
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Date:
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03-Aug-09
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Release date:
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25-Aug-10
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PROCHECK
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Headers
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References
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P0A6L4
(NANA_ECOLI) -
N-acetylneuraminate lyase from Escherichia coli (strain K12)
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Seq:
Struc:
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297 a.a.
302 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 3 residue positions (black
crosses)
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Enzyme class:
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E.C.4.1.3.3
- N-acetylneuraminate lyase.
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Reaction:
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aceneuramate = aldehydo-N-acetyl-D-mannosamine + pyruvate
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aceneuramate
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=
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aldehydo-N-acetyl-D-mannosamine
Bound ligand (Het Group name = )
matches with 50.00% similarity
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+
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pyruvate
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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J Mol Biol
404:56-69
(2010)
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PubMed id:
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Structural insights into substrate specificity in variants of N-acetylneuraminic Acid lyase produced by directed evolution.
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I.Campeotto,
A.H.Bolt,
T.A.Harman,
C.Dennis,
C.H.Trinh,
S.E.Phillips,
A.Nelson,
A.R.Pearson,
A.Berry.
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ABSTRACT
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Links
