1zg6

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{{STRUCTURE_1zg6| PDB=1zg6 | SCENE= }}
{{STRUCTURE_1zg6| PDB=1zg6 | SCENE= }}
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'''TEM1 beta lactamase mutant S70G'''
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===TEM1 beta lactamase mutant S70G===
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==Overview==
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One of the best-studied examples of a class A beta-lactamase is Escherichia coli TEM-1 beta-lactamase. In this class of enzymes, the active-site serine residue takes on the role of a nucleophile and carries out beta-lactam hydrolysis. Here, the structures of the wild-type and the S70G enzyme determined to 1.55 and 2.1 A, respectively, are presented. In contrast to the previously reported 1.8 A structure, the active site of the wild-type enzyme (1.55 A) structure does not contain sulfate and Ser70 appears to be in the deprotonated form. The X-ray crystal structure of the S70G mutant has an altered Ser130 side-chain conformation that influences the positions of water molecules in the active site. This change allows an additional water molecule to be positioned similarly to the serine hydroxyl in the wild-type enzyme. The structure of the mutant enzyme suggests that this water molecule can assume the role of an active-site nucleophile and carry out noncovalent catalysis. The drop in activity in the mutant enzyme is comparable to the drop observed in an analogous mutation of the nucleophilic serine in alkaline phosphatase, suggesting common chemical principles in the utilization of nucleophilic serine in the active site of different enzymes.
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(as it appears on PubMed at http://www.pubmed.gov), where 16041072 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16041072}}
==About this Structure==
==About this Structure==
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[[Category: Wojciechowski, C L.]]
[[Category: Wojciechowski, C L.]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 02:21:23 2008''

Revision as of 23:21, 28 July 2008

Image:1zg6.png

Template:STRUCTURE 1zg6

TEM1 beta lactamase mutant S70G

Template:ABSTRACT PUBMED 16041072

About this Structure

1ZG6 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Structure of the wild-type TEM-1 beta-lactamase at 1.55 A and the mutant enzyme Ser70Ala at 2.1 A suggest the mode of noncovalent catalysis for the mutant enzyme., Stec B, Holtz KM, Wojciechowski CL, Kantrowitz ER, Acta Crystallogr D Biol Crystallogr. 2005 Aug;61(Pt 8):1072-9. Epub 2005, Jul 20. PMID:16041072

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