3a3j
From Proteopedia
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==Crystal structures of penicillin binding protein 5 from Haemophilus influenzae== | ==Crystal structures of penicillin binding protein 5 from Haemophilus influenzae== | ||
| - | <StructureSection load='3a3j' size='340' side='right' caption='[[3a3j]], [[Resolution|resolution]] 2.15Å' scene=''> | + | <StructureSection load='3a3j' size='340' side='right'caption='[[3a3j]], [[Resolution|resolution]] 2.15Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3a3j]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3a3j]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A3J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3A3J 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]] 2.15Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=3a3j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a3j OCA], [https://pdbe.org/3a3j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3a3j RCSB], [https://www.ebi.ac.uk/pdbsum/3a3j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3a3j ProSAT]</span></td></tr> | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/DACA_HAEIN DACA_HAEIN] Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors. | ||
== 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=3a3j 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=3a3j ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | We have determined high-resolution apo crystal structures of two low molecular weight penicillin-binding proteins (PBPs), PBP4 and PBP5, from Haemophilus influenzae, one of the most frequently found pathogens in the upper respiratory tract of children. Novel beta-lactams with notable antimicrobial activity have been designed, and crystal structures of PBP4 complexed with ampicillin and two of the novel molecules have also been determined. Comparing the apo form with those of the complexes, we find that the drugs disturb the PBP4 structure and weaken X-ray diffraction, to very different extents. PBP4 has recently been shown to act as a sensor of the presence of penicillins in Pseudomonas aeruginosa, and our models offer a clue to the structural basis for this effect. Covalently attached penicillins press against a phenylalanine residue near the active site and disturb the deacylation step. The ready inhibition of PBP4 by beta-lactams compared to PBP5 also appears to be related to the weaker interactions holding key residues in a catalytically competent position. | ||
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| - | Crystal structures of penicillin-binding proteins 4 and 5 from Haemophilus influenzae.,Kawai F, Clarke TB, Roper DI, Han GJ, Hwang KY, Unzai S, Obayashi E, Park SY, Tame JR J Mol Biol. 2010 Feb 26;396(3):634-45. Epub 2009 Dec 1. PMID:19958776<ref>PMID:19958776</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 3a3j" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
| - | *[[Penicillin-binding protein|Penicillin-binding protein]] | + | *[[Penicillin-binding protein 3D structures|Penicillin-binding protein 3D structures]] |
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Haemophilus influenzae]] |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Kawai | + | [[Category: Kawai F]] |
| - | [[Category: Park | + | [[Category: Park S-Y]] |
| - | [[Category: Roper | + | [[Category: Roper DI]] |
| - | [[Category: Tame | + | [[Category: Tame JRH]] |
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Current revision
Crystal structures of penicillin binding protein 5 from Haemophilus influenzae
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