We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

3dw0

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
{{STRUCTURE_3dw0| PDB=3dw0 | SCENE= }}
+
==Crystal structure of the class A carbapenemase KPC-2 at 1.6 angstrom resolution==
-
===Crystal structure of the class A carbapenemase KPC-2 at 1.6 angstrom resolution===
+
<StructureSection load='3dw0' size='340' side='right' caption='[[3dw0]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
-
{{ABSTRACT_PUBMED_18625772}}
+
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[3dw0]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2ods 2ods]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DW0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3DW0 FirstGlance]. <br>
 +
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3dw0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dw0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3dw0 RCSB], [http://www.ebi.ac.uk/pdbsum/3dw0 PDBsum]</span></td></tr>
 +
</table>
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dw/3dw0_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Two clinical strains of Escherichia coli (2138) and Enterobacter cloacae (7506) isolated from the same patient in France and showing resistance to extended-spectrum cephalosporins and low susceptibility to imipenem were investigated. Both strains harbored the plasmid-contained bla(TEM-1) and bla(KPC-2) genes. bla(KLUC-2), encoding a mutant of the chromosomal beta-lactamase of Kluyvera cryocrescens, was also identified at a plasmid location in E. cloacae 7506, suggesting the ISEcp1-assisted escape of bla(KLUC) from the chromosome. Determination of the KPC-2 structure at 1.6 A revealed that the binding site was occupied by the C-terminal (C-ter) residues coming from a symmetric KPC-2 monomer, with the ultimate C-ter Glu interacting with Ser130, Lys234, Thr235, and Thr237 in the active site. This mode of binding can be paralleled to the inhibition of the TEM-1 beta-lactamase by the inhibitory protein BLIP. Determination of the 1.23-A structure of a KPC-2 mutant in which the five C-ter residues were deleted revealed that the catalytic site was filled by a citrate molecule. Structure analysis and docking simulations with cefotaxime and imipenem provided further insights into the molecular basis of the extremely broad spectrum of KPC-2, which behaves as a cefotaximase with significant activity against carbapenems. In particular, residues 104, 105, 132, and 167 draw a binding cavity capable of accommodating both the aminothiazole moiety of cefotaxime and the 6 alpha-hydroxyethyl group of imipenem, with the binding of the former drug being also favored by a significant degree of freedom at the level of the loop at positions 96 to 105 and by an enlargement of the binding site at the end of strand beta 3.
-
==About this Structure==
+
Genetic and structural insights into the dissemination potential of the extremely broad-spectrum class A beta-lactamase KPC-2 identified in an Escherichia coli strain and an Enterobacter cloacae strain isolated from the same patient in France.,Petrella S, Ziental-Gelus N, Mayer C, Renard M, Jarlier V, Sougakoff W Antimicrob Agents Chemother. 2008 Oct;52(10):3725-36. Epub 2008 Jul 14. PMID:18625772<ref>PMID:18625772</ref>
-
[[3dw0]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2ods 2ods]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DW0 OCA].
+
-
==Reference==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
<ref group="xtra">PMID:018625772</ref><references group="xtra"/><references/>
+
</div>
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
-
[[Category: Jarlier, V.]]
+
[[Category: Jarlier, V]]
-
[[Category: Mayer, C.]]
+
[[Category: Mayer, C]]
-
[[Category: Petrella, S.]]
+
[[Category: Petrella, S]]
-
[[Category: Sougakoff, W.]]
+
[[Category: Sougakoff, W]]
-
[[Category: Ziental-Gelus, N.]]
+
[[Category: Ziental-Gelus, N]]
[[Category: Antibiotic resistance]]
[[Category: Antibiotic resistance]]
[[Category: Beta-lactamase]]
[[Category: Beta-lactamase]]

Revision as of 18:28, 21 December 2014

Crystal structure of the class A carbapenemase KPC-2 at 1.6 angstrom resolution

3dw0, resolution 1.60Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3dw0"
Personal tools