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| | <StructureSection load='1e25' size='340' side='right'caption='[[1e25]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='1e25' size='340' side='right'caption='[[1e25]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1e25]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E25 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1E25 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1e25]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E25 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E25 FirstGlance]. <br> |
| - | </td></tr><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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BLAPER-1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 "Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885])</td></tr> | + | <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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-lactamase Beta-lactamase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.6 3.5.2.6] </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=1e25 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e25 OCA], [https://pdbe.org/1e25 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e25 RCSB], [https://www.ebi.ac.uk/pdbsum/1e25 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e25 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1e25 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e25 OCA], [http://pdbe.org/1e25 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1e25 RCSB], [http://www.ebi.ac.uk/pdbsum/1e25 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1e25 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/BLE1_PSEAI BLE1_PSEAI] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Beta-lactamase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bouthors, A T]] | + | [[Category: Pseudomonas aeruginosa]] |
| - | [[Category: Guillet, V]] | + | [[Category: Bouthors AT]] |
| - | [[Category: Maveyraud, L]] | + | [[Category: Guillet V]] |
| - | [[Category: Samama, J P]] | + | [[Category: Maveyraud L]] |
| - | [[Category: Sougakoff, W]] | + | [[Category: Samama JP]] |
| - | [[Category: Tranier, S]] | + | [[Category: Sougakoff W]] |
| - | [[Category: Antibiotic resistance]]
| + | [[Category: Tranier S]] |
| - | [[Category: Class a cephalosporinase]]
| + | |
| - | [[Category: Hydrolase]]
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| Structural highlights
Function
BLE1_PSEAI
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The treatment of infectious diseases by beta-lactam antibiotics is continuously challenged by the emergence and dissemination of new beta-lactamases. In most cases, the cephalosporinase activity of class A enzymes results from a few mutations in the TEM and SHV penicillinases. The PER-1 beta-lactamase was characterized as a class A enzyme displaying a cephalosporinase activity. This activity was, however, insensitive to the mutations of residues known to be critical for providing extended substrate profiles to TEM and SHV. The x-ray structure of the protein, solved at 1.9-A resolution, reveals that two of the most conserved features in class A beta-lactamases are not present in this enzyme: the fold of the Omega-loop and the cis conformation of the peptide bond between residues 166 and 167. The new fold of the Omega-loop and the insertion of four residues at the edge of strand S3 generate a broad cavity that may easily accommodate the bulky substituents of cephalosporin substrates. The trans conformation of the 166-167 bond is related to the presence of an aspartic acid at position 136. Selection of class A enzymes based on the occurrence of both Asp(136) and Asn(179) identifies a subgroup of enzymes with high sequence homology.
The high resolution crystal structure for class A beta-lactamase PER-1 reveals the bases for its increase in breadth of activity.,Tranier S, Bouthors AT, Maveyraud L, Guillet V, Sougakoff W, Samama JP J Biol Chem. 2000 Sep 8;275(36):28075-82. PMID:10825176[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Tranier S, Bouthors AT, Maveyraud L, Guillet V, Sougakoff W, Samama JP. The high resolution crystal structure for class A beta-lactamase PER-1 reveals the bases for its increase in breadth of activity. J Biol Chem. 2000 Sep 8;275(36):28075-82. PMID:10825176 doi:http://dx.doi.org/10.1074/jbc.M003802200
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