2exb: Difference between revisions

Revision as of 09:34, 29 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:2exb.png

Template:STRUCTURE 2exb

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

Template:ABSTRACT PUBMED 16411754

About this StructureAbout this Structure

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

ReferenceReference

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

Page seeded by OCA on Tue Jul 29 09:34:47 2008

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

OCA

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-'''Crystal structure of penicillin binding protein 4 (dacB) from Escherichia coli, complexed with FLOMOX'''
+===Crystal structure of penicillin binding protein 4 (dacB) from Escherichia coli, complexed with FLOMOX===
-==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.
+The line below this paragraph, {{ABSTRACT_PUBMED_16411754}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_16411754}}
 ==About this Structure==
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 [[Category: Penicillin]]
 [[Category: Penicillin-binding protein]]
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