2ov5

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (08:25, 30 October 2024) (edit) (undo)
 
(11 intermediate revisions not shown.)
Line 1: Line 1:
-
{{Seed}}
 
-
[[Image:2ov5.png|left|200px]]
 
-
<!--
+
==Crystal structure of the KPC-2 carbapenemase==
-
The line below this paragraph, containing "STRUCTURE_2ov5", creates the "Structure Box" on the page.
+
<StructureSection load='2ov5' size='340' side='right'caption='[[2ov5]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<table><tr><td colspan='2'>[[2ov5]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Klebsiella_pneumoniae Klebsiella pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OV5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OV5 FirstGlance]. <br>
-
or leave the SCENE parameter empty for the default display.
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85&#8491;</td></tr>
-
-->
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BCN:BICINE'>BCN</scene></td></tr>
-
{{STRUCTURE_2ov5| PDB=2ov5 | SCENE= }}
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ov5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ov5 OCA], [https://pdbe.org/2ov5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ov5 RCSB], [https://www.ebi.ac.uk/pdbsum/2ov5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ov5 ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/BLKPC_KLEPN BLKPC_KLEPN] Hydrolyzes carbapenems, penicillins, cephalosporins and monobactams with varying efficiency.
 +
== 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/ov/2ov5_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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/main_output.php?pdb_ID=2ov5 ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Beta-lactamases inactivate beta-lactam antibiotics and are a major cause of antibiotic resistance. The recent outbreaks of Klebsiella pneumoniae carbapenem resistant (KPC) infections mediated by KPC type beta-lactamases are creating a serious threat to our "last resort" antibiotics, the carbapenems. KPC beta-lactamases are serine carbapenemases and are a subclass of class A beta-lactamases that have evolved to efficiently hydrolyze carbapenems and cephamycins which contain substitutions at the alpha-position proximal to the carbonyl group that normally render these beta-lactams resistant to hydrolysis. To investigate the molecular basis of this carbapenemase activity, we have determined the structure of KPC-2 at 1.85 A resolution. The active site of KPC-2 reveals the presence of a bicine buffer molecule which interacts via its carboxyl group with conserved active site residues S130, K234, T235, and T237; these likely resemble the interactions the beta-lactam carboxyl moiety makes in the Michaelis-Menten complex. Comparison of the KPC-2 structure with non-carbapenemases and previously determined NMC-A and SME-1 carbapenemase structures shows several active site alterations that are unique among carbapenemases. An outward shift of the catalytic S70 residue renders the active sites of the carbapenemases more shallow, likely allowing easier access of the bulkier substrates. Further space for the alpha-substituents is potentially provided by shifts in N132 and N170 in addition to concerted movements in the postulated carboxyl binding pocket that might allow the substrates to bind at a slightly different angle to accommodate these alpha-substituents. The structure of KPC-2 provides key insights into the carbapenemase activity of emerging class A beta-lactamases.
-
===Crystal structure of the KPC-2 carbapenemase===
+
Crystal structure of KPC-2: insights into carbapenemase activity in class A beta-lactamases.,Ke W, Bethel CR, Thomson JM, Bonomo RA, van den Akker F Biochemistry. 2007 May 15;46(19):5732-40. Epub 2007 Apr 19. PMID:17441734<ref>PMID:17441734</ref>
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 2ov5" style="background-color:#fffaf0;"></div>
-
<!--
+
==See Also==
-
The line below this paragraph, {{ABSTRACT_PUBMED_17441734}}, adds the Publication Abstract to the page
+
*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]]
-
(as it appears on PubMed at http://www.pubmed.gov), where 17441734 is the PubMed ID number.
+
== References ==
-
-->
+
<references/>
-
{{ABSTRACT_PUBMED_17441734}}
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
-
2OV5 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Klebsiella_pneumoniae Klebsiella pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OV5 OCA].
+
-
 
+
-
==Reference==
+
-
Crystal structure of KPC-2: insights into carbapenemase activity in class A beta-lactamases., Ke W, Bethel CR, Thomson JM, Bonomo RA, van den Akker F, Biochemistry. 2007 May 15;46(19):5732-40. Epub 2007 Apr 19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17441734 17441734]
+
-
[[Category: Beta-lactamase]]
+
[[Category: Klebsiella pneumoniae]]
[[Category: Klebsiella pneumoniae]]
-
[[Category: Single protein]]
+
[[Category: Large Structures]]
-
[[Category: Akker, F van den.]]
+
[[Category: Bethel CR]]
-
[[Category: Bethel, C R.]]
+
[[Category: Bonomo RA]]
-
[[Category: Bonomo, R A.]]
+
[[Category: Ke W]]
-
[[Category: Ke, W.]]
+
[[Category: Thomson JM]]
-
[[Category: Thomson, J M.]]
+
[[Category: Van den Akker F]]
-
[[Category: Beta-lactamase]]
+
-
[[Category: Carbapenemase]]
+
-
[[Category: Hydrolase]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Nov 19 20:18:22 2008''
+

Current revision

Crystal structure of the KPC-2 carbapenemase

PDB ID 2ov5

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/2ov5"
Personal tools