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1hzo

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[[Image:1hzo.jpg|left|200px]]
 
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{{Structure
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==STRUCTURE OF CLASS A CEPHALOSPORINASE FROM PROTEUS VULGARIS K1==
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|PDB= 1hzo |SIZE=350|CAPTION= <scene name='initialview01'>1hzo</scene>, resolution 1.75&Aring;
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<StructureSection load='1hzo' size='340' side='right'caption='[[1hzo]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC ACID'>MES</scene>
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<table><tr><td colspan='2'>[[1hzo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Proteus_vulgaris Proteus vulgaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HZO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HZO FirstGlance]. <br>
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|ACTIVITY= [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]
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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]] 1.75&#8491;</td></tr>
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|GENE= BLAC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=585 Proteus vulgaris])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene></td></tr>
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}}
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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=1hzo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hzo OCA], [https://pdbe.org/1hzo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hzo RCSB], [https://www.ebi.ac.uk/pdbsum/1hzo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hzo ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/BLAB_PROVU BLAB_PROVU] Hydrolyzes broad-spectrum beta-lactam antibiotics. Active against cephalosporins such as cefuroxime and cefotaxime.
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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/hz/1hzo_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=1hzo 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 structure of a chromosomal extended-spectrum beta-lactamase (ESBL) having the ability to hydrolyze cephalosporins including cefuroxime and ceftazidime has been determined by X-ray crystallography to 1.75 A resolution. The species-specific class A beta-lactamase from Proteus vulgaris K1 was crystallized at pH 6.25 and its structure solved by molecular replacement. Refinement of the model resulted in crystallographic R and R(free) of 16.9 % and 19.3 %, respectively. The folding of the K1 enzyme is broadly similar to that of non-ESBL TEM-type beta-lactamases (2 A rmsd for C(alpha)) and differs by only 0.35 A for all atoms of six conserved residues in the catalytic site. Other residues promoting extended-spectrum activity in K1 include the side-chains of atypical residues Ser237 and Lys276. These side-chains are linked by two water molecules, one of which lies in the position normally filled by the guanidinium group of Arg244, present in most non-ESBL enzymes but absent from K1. The ammonium group of Lys276, ca 3.5 A from the virtual Arg244 guanidinium position, may interact with polar R2 substitutents on the dihydrothiazene ring of cephalosporins.
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'''STRUCTURE OF CLASS A CEPHALOSPORINASE FROM PROTEUS VULGARIS K1'''
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Structure of an extended-spectrum class A beta-lactamase from Proteus vulgaris K1.,Nukaga M, Mayama K, Crichlow GV, Knox JR J Mol Biol. 2002 Mar 15;317(1):109-17. PMID:11916382<ref>PMID:11916382</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 1hzo" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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The structure of a chromosomal extended-spectrum beta-lactamase (ESBL) having the ability to hydrolyze cephalosporins including cefuroxime and ceftazidime has been determined by X-ray crystallography to 1.75 A resolution. The species-specific class A beta-lactamase from Proteus vulgaris K1 was crystallized at pH 6.25 and its structure solved by molecular replacement. Refinement of the model resulted in crystallographic R and R(free) of 16.9 % and 19.3 %, respectively. The folding of the K1 enzyme is broadly similar to that of non-ESBL TEM-type beta-lactamases (2 A rmsd for C(alpha)) and differs by only 0.35 A for all atoms of six conserved residues in the catalytic site. Other residues promoting extended-spectrum activity in K1 include the side-chains of atypical residues Ser237 and Lys276. These side-chains are linked by two water molecules, one of which lies in the position normally filled by the guanidinium group of Arg244, present in most non-ESBL enzymes but absent from K1. The ammonium group of Lys276, ca 3.5 A from the virtual Arg244 guanidinium position, may interact with polar R2 substitutents on the dihydrothiazene ring of cephalosporins.
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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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1HZO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Proteus_vulgaris Proteus vulgaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HZO 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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Structure of an extended-spectrum class A beta-lactamase from Proteus vulgaris K1., Nukaga M, Mayama K, Crichlow GV, Knox JR, J Mol Biol. 2002 Mar 15;317(1):109-17. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11916382 11916382]
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[[Category: Beta-lactamase]]
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[[Category: Proteus vulgaris]]
[[Category: Proteus vulgaris]]
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[[Category: Single protein]]
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[[Category: Crichlow GV]]
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[[Category: Crichlow, G V.]]
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[[Category: Knox JR]]
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[[Category: Knox, J R.]]
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[[Category: Kuzin AP]]
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[[Category: Kuzin, A P.]]
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[[Category: Mayama K]]
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[[Category: Mayama, K.]]
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[[Category: Nukaga M]]
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[[Category: Nukaga, M.]]
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[[Category: MES]]
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[[Category: cephalosporinase]]
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[[Category: class a beta-lactamase]]
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[[Category: hydrolase]]
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[[Category: mixed alpha/beta]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:43:40 2008''
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Current revision

STRUCTURE OF CLASS A CEPHALOSPORINASE FROM PROTEUS VULGARIS K1

PDB ID 1hzo

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