1k25: Difference between revisions

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-[[Image:1k25.jpg|left|200px]]
- {{Structure
+==PBP2x from a Highly Penicillin-resistant Streptococcus pneumoniae Clinical Isolate==
-|PDB= 1k25 |SIZE=350|CAPTION= <scene name='initialview01'>1k25</scene>, resolution 3.20&Aring;
+<StructureSection load='1k25' size='340' side='right'caption='[[1k25]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND=
+<table><tr><td colspan='2'>[[1k25]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pneumoniae Streptococcus pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K25 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1K25 FirstGlance]. <br>
-|ACTIVITY=
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.2&#8491;</td></tr>
-|GENE=
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1k25 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k25 OCA], [https://pdbe.org/1k25 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1k25 RCSB], [https://www.ebi.ac.uk/pdbsum/1k25 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1k25 ProSAT]</span></td></tr>
-|DOMAIN=
+</table>
-|RELATEDENTRY=[[1qmf|1QMF]], [[1qme|1QME]]
+== Function ==
-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1k25 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k25 OCA], [http://www.ebi.ac.uk/pdbsum/1k25 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1k25 RCSB]</span>
+[https://www.uniprot.org/uniprot/O34006_STREE O34006_STREE]
-}}
+== 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/k2/1k25_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/main_output.php?pdb_ID=1k25 ConSurf].
+<div style="clear:both"></div>
-'''PBP2x from a Highly Penicillin-resistant Streptococcus pneumoniae Clinical Isolate'''
+==See Also==
+*[[Penicillin-binding protein 3D structures|Penicillin-binding protein 3D structures]]
+__TOC__
-==Overview==
+</StructureSection>
-Penicillin-binding proteins (PBPs) are the main targets for beta-lactam antibiotics, such as penicillins and cephalosporins, in a wide range of bacterial species. In some Gram-positive strains, the surge of resistance to treatment with beta-lactams is primarily the result of the proliferation of mosaic PBP-encoding genes, which encode novel proteins by recombination. PBP2x is a primary resistance determinant in Streptococcus pneumoniae, and its modification is an essential step in the development of high level beta-lactam resistance. To understand such a resistance mechanism at an atomic level, we have solved the x-ray crystal structure of PBP2x from a highly penicillin-resistant clinical isolate of S. pneumoniae, Sp328, which harbors 83 mutations in the soluble region. In the proximity of the Sp328 PBP2x* active site, the Thr(338) --&gt; Ala mutation weakens the local hydrogen bonding network, thus abrogating the stabilization of a crucial buried water molecule. In addition, the Ser(389) --&gt; Leu and Asn(514) --&gt; His mutations produce a destabilizing effect that generates an "open" active site. It has been suggested that peptidoglycan substrates for beta-lactam-resistant PBPs contain a large amount of abnormal, branched peptides, whereas sensitive strains tend to catalyze cross-linking of linear forms. Thus, in vivo, an "open" active site could facilitate the recognition of distinct, branched physiological substrates.
+[[Category: Large Structures]]
-==About this Structure==
-K25 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_pneumoniae Streptococcus pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K25 OCA].
-==Reference==
-Crystal structure of PBP2x from a highly penicillin-resistant Streptococcus pneumoniae clinical isolate: a mosaic framework containing 83 mutations., Dessen A, Mouz N, Gordon E, Hopkins J, Dideberg O, J Biol Chem. 2001 Nov 30;276(48):45106-12. Epub 2001 Sep 11. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11553637 11553637]
-[[Category: Single protein]]
 [[Category: Streptococcus pneumoniae]]
-[[Category: Dessen, A.]]
+[[Category: Dessen A]]
-[[Category: Dideberg, O.]]
+[[Category: Dideberg O]]
-[[Category: Hopkins, J.]]
+[[Category: Hopkins J]]
-[[Category: Mouz, N.]]
+[[Category: Mouz N]]
-[[Category: antibiotic resistance]]
-[[Category: clinical mutant]]
-[[Category: low-affinity penicillin-binding]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:42:15 2008''