1mwr
From Proteopedia
(Difference between revisions)
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<StructureSection load='1mwr' size='340' side='right'caption='[[1mwr]], [[Resolution|resolution]] 2.45Å' scene=''> | <StructureSection load='1mwr' size='340' side='right'caption='[[1mwr]], [[Resolution|resolution]] 2.45Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1mwr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1mwr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MWR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MWR FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.45Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1mwr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mwr OCA], [https://pdbe.org/1mwr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mwr RCSB], [https://www.ebi.ac.uk/pdbsum/1mwr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mwr ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1mwr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mwr OCA], [https://pdbe.org/1mwr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mwr RCSB], [https://www.ebi.ac.uk/pdbsum/1mwr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mwr ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q93IC2_STAAU Q93IC2_STAAU] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</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=1mwr ConSurf]. | </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=1mwr ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The multiple antibiotic resistance of methicillin-resistant strains of Staphylococcus aureus (MRSA) has become a major clinical problem worldwide. The key determinant of the broad-spectrum beta-lactam resistance in MRSA strains is the penicillin-binding protein 2a (PBP2a). Because of its low affinity for beta-lactams, PBP2a provides transpeptidase activity to allow cell wall synthesis at beta-lactam concentrations that inhibit the beta-lactam-sensitive PBPs normally produced by S. aureus. The crystal structure of a soluble derivative of PBP2a has been determined to 1.8 A resolution and provides the highest resolution structure for a high molecular mass PBP. Additionally, structures of the acyl-PBP complexes of PBP2a with nitrocefin, penicillin G and methicillin allow, for the first time, a comparison of an apo and acylated resistant PBP. An analysis of the PBP2a active site in these forms reveals the structural basis of its resistance and identifies features in newly developed beta-lactams that are likely important for high affinity binding. | ||
| - | |||
| - | Structural basis for the beta lactam resistance of PBP2a from methicillin-resistant Staphylococcus aureus.,Lim D, Strynadka NC Nat Struct Biol. 2002 Nov;9(11):870-6. PMID:12389036<ref>PMID:12389036</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1mwr" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Penicillin-binding protein 3D structures|Penicillin-binding protein 3D structures]] | *[[Penicillin-binding protein 3D structures|Penicillin-binding protein 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Staphylococcus aureus]] |
| - | [[Category: | + | [[Category: Lim DC]] |
| - | [[Category: | + | [[Category: Strynadka NCJ]] |
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Revision as of 08:42, 10 April 2024
Structure of SeMet Penicillin binding protein 2a from methicillin resistant Staphylococcus aureus strain 27r (trigonal form) at 2.45 A resolution.
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