2ex8

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[[Image:2ex8.gif|left|200px]]
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{{STRUCTURE_2ex8| PDB=2ex8 | SCENE= }}
{{STRUCTURE_2ex8| PDB=2ex8 | SCENE= }}
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'''Crystal structure of penicillin binding protein 4 (dacB) from Escherichia coli, complexed with penicillin-G'''
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===Crystal structure of penicillin binding protein 4 (dacB) from Escherichia coli, complexed with penicillin-G===
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==Overview==
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The crystal structure of penicillin binding protein 4 (PBP4) from Escherichia coli, which has both DD-endopeptidase and DD-carboxypeptidase activity, is presented. PBP4 is one of 12 penicillin binding proteins in E. coli involved in the synthesis and maintenance of the cell wall. The model contains a penicillin binding domain similar to known structures, but includes a large insertion which folds into domains with unique folds. The structures of the protein covalently attached to five different antibiotics presented here show the active site residues are unmoved compared to the apoprotein, but nearby surface loops and helices are displaced in some cases. The altered geometry of conserved active site residues compared with those of other PBPs suggests a possible cause for the slow deacylation rate of PBP4.
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(as it appears on PubMed at http://www.pubmed.gov), where 16411754 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16411754}}
==About this Structure==
==About this Structure==
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[[Category: Penicillin-binding protein]]
[[Category: Penicillin-binding protein]]
[[Category: Penicillin-g]]
[[Category: Penicillin-g]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 13:23:24 2008''

Revision as of 10:23, 28 July 2008

Image:2ex8.png

Template:STRUCTURE 2ex8

Crystal structure of penicillin binding protein 4 (dacB) from Escherichia coli, complexed with penicillin-G

Template:ABSTRACT PUBMED 16411754

About this Structure

2EX8 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Crystal structure of penicillin binding protein 4 (dacB) from Escherichia coli, both in the native form and covalently linked to various antibiotics., Kishida H, Unzai S, Roper DI, Lloyd A, Park SY, Tame JR, Biochemistry. 2006 Jan 24;45(3):783-92. PMID:16411754

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