1pmd
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1pmd]] is a 1 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=1PMD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PMD FirstGlance]. <br> | <table><tr><td colspan='2'>[[1pmd]] is a 1 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=1PMD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PMD FirstGlance]. <br> | ||
| - | </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=1pmd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pmd OCA], [https://pdbe.org/1pmd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pmd RCSB], [https://www.ebi.ac.uk/pdbsum/1pmd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pmd ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.5Å</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=1pmd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pmd OCA], [https://pdbe.org/1pmd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pmd RCSB], [https://www.ebi.ac.uk/pdbsum/1pmd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pmd ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/PBPX_STRPN PBPX_STRPN] Penicillin-binding proteins (PBPs) function in the late steps of murein biosynthesis. Beta-lactams inactivate the PBPs by acylating an essential serine residue in the active site of these proteins. | |
== 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=1pmd 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=1pmd ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | All beta-lactam antibiotics exert their biological effects by interacting with a unique class of proteins, the penicillin-binding proteins (PBPs). These membrane proteins are involved in the biosynthesis of the murein or peptidoglycan, a mesh-like structure which completely surrounds the bacterial cell. Sequence similarities indicate that one domain of these proteins belongs to a large family of beta-lactam-recognizing proteins, which includes the active-site serine beta-lactamases. We here report the first three-dimensional crystal structure of a high molecular weight penicillin-binding protein, PBP2x of Streptococcus pneumoniae, at 3.5 A resolution. The molecule has three domains, the central domain being a transpeptidase, which is a suitable target for antibiotic development. | ||
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| - | X-ray structure of Streptococcus pneumoniae PBP2x, a primary penicillin target enzyme.,Pares S, Mouz N, Petillot Y, Hakenbeck R, Dideberg O Nat Struct Biol. 1996 Mar;3(3):284-9. PMID:8605631<ref>PMID:8605631</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1pmd" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Streptococcus pneumoniae]] | [[Category: Streptococcus pneumoniae]] | ||
| - | [[Category: Dideberg | + | [[Category: Dideberg O]] |
| - | [[Category: Mouz | + | [[Category: Mouz N]] |
| - | [[Category: Pares | + | [[Category: Pares S]] |
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Current revision
PENICILLIN-BINDING PROTEIN 2X (PBP-2X)
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