2exb: Difference between revisions

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[[Image:2exb.gif|left|200px]]<br /><applet load="2exb" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:2exb.gif|left|200px]]
caption="2exb, resolution 1.75&Aring;" />
 
'''Crystal structure of penicillin binding protein 4 (dacB) from Escherichia coli, complexed with FLOMOX'''<br />
{{Structure
|PDB= 2exb |SIZE=350|CAPTION= <scene name='initialview01'>2exb</scene>, resolution 1.75&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=FXM:2,2-DIMETHYLPROPANOYLOXYMETHYL+(6R,7R)-7-[(Z)-2-(2-AMINOTHIAZOL-4-YL)PENT-2-ENYLAMINO]-3-CARBAMOYLOXYMETHYL-8-OXO-5-THIA-1-AZABICYCLO[4.2.0]OCT-2-ENE-2-CARBOXYLATE'>FXM</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
|ACTIVITY=
|GENE= dacb ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
}}
 
'''Crystal structure of penicillin binding protein 4 (dacB) from Escherichia coli, complexed with FLOMOX'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
2EXB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=FXM:'>FXM</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EXB OCA].  
2EXB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EXB OCA].  


==Reference==
==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16411754 16411754]
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:[http://www.ncbi.nlm.nih.gov/pubmed/16411754 16411754]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: penicillin-binding protein]]
[[Category: penicillin-binding protein]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:15:29 2008''
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Revision as of 17:45, 20 March 2008

File:2exb.gif


PDB ID 2exb

Drag the structure with the mouse to rotate
, resolution 1.75Å
Ligands: and
Gene: dacb (Escherichia coli)
Coordinates: save as pdb, mmCIF, xml



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


OverviewOverview

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.

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

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