2exa: Difference between revisions

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[[Image:2exa.~~gif~~|left|200px]]

[[Image:2exa.png|left|200px]]

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~~'''~~Crystal structure of penicillin binding protein 4 (dacB) from Escherichia coli, complexed with FAROM~~'''~~

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

~~==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

(as it appears on PubMed at http://www.pubmed.gov), where 16411754 is the PubMed ID number.

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==About this Structure==

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[[Category: Penicillin,cephem]]

[[Category: Penicillin-binding protein]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun ~~May 4 03~~:13:05 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 12:27:25 2008''

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-[[Image:2exa.gif|left|200px]]
+{{Seed}}
+[[Image:2exa.png|left|200px]]
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 {{STRUCTURE_2exa|  PDB=2exa  |  SCENE=  }}
-'''Crystal structure of penicillin binding protein 4 (dacB) from Escherichia coli, complexed with FAROM'''
+===Crystal structure of penicillin binding protein 4 (dacB) from Escherichia coli, complexed with FAROM===
-==Overview==
+<!--
-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
+(as it appears on PubMed at http://www.pubmed.gov), where 16411754 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16411754}}
 ==About this Structure==
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 [[Category: Penicillin,cephem]]
 [[Category: Penicillin-binding protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 03:13:05 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 12:27:25 2008''