2b9v: Difference between revisions

Revision as of 18:37, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2b9v.png

Template:STRUCTURE 2b9v

Acetobacter turbidans alpha-amino acid ester hydrolaseAcetobacter turbidans alpha-amino acid ester hydrolase

Template:ABSTRACT PUBMED 16377627

About this StructureAbout this Structure

2B9V is a Single protein structure of sequence from Acetobacter pasteurianus. Full crystallographic information is available from OCA.

ReferenceReference

Acetobacter turbidans alpha-amino acid ester hydrolase: how a single mutation improves an antibiotic-producing enzyme., Barends TR, Polderman-Tijmes JJ, Jekel PA, Williams C, Wybenga G, Janssen DB, Dijkstra BW, J Biol Chem. 2006 Mar 3;281(9):5804-10. Epub 2005 Dec 23. PMID:16377627

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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 {{STRUCTURE_2b9v|  PDB=2b9v  |  SCENE=  }}
-'''Acetobacter turbidans alpha-amino acid ester hydrolase'''
+===Acetobacter turbidans alpha-amino acid ester hydrolase===
-==Overview==
+<!--
-The alpha-amino acid ester hydrolase (AEH) from Acetobacter turbidans is a bacterial enzyme catalyzing the hydrolysis and synthesis of beta-lactam antibiotics. The crystal structures of the native enzyme, both unliganded and in complex with the hydrolysis product D-phenylglycine are reported, as well as the structures of an inactive mutant (S205A) complexed with the substrate ampicillin, and an active site mutant (Y206A) with an increased tendency to catalyze antibiotic production rather than hydrolysis. The structure of the native enzyme shows an acyl binding pocket, in which D-phenylglycine binds, and an additional space that is large enough to accommodate the beta-lactam moiety of an antibiotic. In the S205A mutant, ampicillin binds in this pocket in a non-productive manner, making extensive contacts with the side chain of Tyr(112), which also participates in oxyanion hole formation. In the Y206A mutant, the Tyr(112) side chain has moved with its hydroxyl group toward the catalytic serine. Because this changes the properties of the beta-lactam binding site, this could explain the increased beta-lactam transferase activity of this mutant.
+The line below this paragraph, {{ABSTRACT_PUBMED_16377627}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16377627 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_16377627}}
 ==About this Structure==
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 [[Category: Alpha/beta-hydrolase]]
 [[Category: Catalytic triad]]
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