2b61

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{{STRUCTURE_2b61| PDB=2b61 | SCENE= }}
{{STRUCTURE_2b61| PDB=2b61 | SCENE= }}
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'''Crystal Structure of Homoserine Transacetylase'''
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===Crystal Structure of Homoserine Transacetylase===
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==Overview==
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Homoserine transacetylase catalyzes one of the required steps in the biosynthesis of methionine in fungi and several bacteria. We have determined the crystal structure of homoserine transacetylase from Haemophilus influenzae to a resolution of 1.65 A. The structure identifies this enzyme to be a member of the alpha/beta-hydrolase structural superfamily. The active site of the enzyme is located near the end of a deep tunnel formed by the juxtaposition of two domains and incorporates a catalytic triad involving Ser143, His337, and Asp304. A structural basis is given for the observed double displacement kinetic mechanism of homoserine transacetylase. Furthermore, the properties of the tunnel provide a rationale for how homoserine transacetylase catalyzes a transferase reaction vs hydrolysis, despite extensive similarity in active site architecture to hydrolytic enzymes.
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(as it appears on PubMed at http://www.pubmed.gov), where 16313180 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16313180}}
==About this Structure==
==About this Structure==
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[[Category: Coenzyme some]]
[[Category: Coenzyme some]]
[[Category: Structure-function study]]
[[Category: Structure-function study]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 04:15:23 2008''

Revision as of 01:15, 29 July 2008

Image:2b61.png

Template:STRUCTURE 2b61

Crystal Structure of Homoserine Transacetylase

Template:ABSTRACT PUBMED 16313180

About this Structure

2B61 is a Single protein structure of sequence from Haemophilus influenzae. Full crystallographic information is available from OCA.

Reference

Crystal structure of homoserine transacetylase from Haemophilus influenzae reveals a new family of alpha/beta-hydrolases., Mirza IA, Nazi I, Korczynska M, Wright GD, Berghuis AM, Biochemistry. 2005 Dec 6;44(48):15768-73. PMID:16313180

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