1e25

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[[Image:1e25.gif|left|200px]]
 
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{{Structure
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==The high resolution structure of PER-1 class A beta-lactamase==
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|PDB= 1e25 |SIZE=350|CAPTION= <scene name='initialview01'>1e25</scene>, resolution 1.90&Aring;
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<StructureSection load='1e25' size='340' side='right'caption='[[1e25]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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<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>
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|ACTIVITY= <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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
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|GENE= BLAPER-1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 Pseudomonas aeruginosa])
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<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>
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|DOMAIN=
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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=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>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1e25 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e25 OCA], [http://www.ebi.ac.uk/pdbsum/1e25 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1e25 RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/BLE1_PSEAI BLE1_PSEAI]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e2/1e25_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1e25 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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'''THE HIGH RESOLUTION STRUCTURE OF PER-1 CLASS A BETA-LACTAMASE'''
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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<ref>PMID:10825176</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1e25" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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.
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*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1E25 is a [[Single protein]] structure of sequence from [http://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].
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Large Structures]]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/10825176 10825176]
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[[Category: Beta-lactamase]]
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[[Category: Pseudomonas aeruginosa]]
[[Category: Pseudomonas aeruginosa]]
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[[Category: Single protein]]
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[[Category: Bouthors AT]]
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[[Category: Bouthors, A T.]]
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[[Category: Guillet V]]
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[[Category: Guillet, V.]]
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[[Category: Maveyraud L]]
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[[Category: Maveyraud, L.]]
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[[Category: Samama JP]]
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[[Category: P, J.]]
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[[Category: Sougakoff W]]
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[[Category: Sougakoff, W.]]
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[[Category: Tranier S]]
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[[Category: Tranier, S.]]
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[[Category: antibiotic resistance]]
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[[Category: class a cephalosporinase]]
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[[Category: hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:53:30 2008''
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Current revision

The high resolution structure of PER-1 class A beta-lactamase

PDB ID 1e25

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