1lqp

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[[Image:1lqp.gif|left|200px]]<br /><applet load="1lqp" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1lqp, resolution 1.19&Aring;" />
 
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'''CRYSTAL STRUCTURE OF THE FOSFOMYCIN RESISTANCE PROTEIN (FOSA) CONTAINING BOUND SUBSTRATE'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF THE FOSFOMYCIN RESISTANCE PROTEIN (FOSA) CONTAINING BOUND SUBSTRATE==
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The fosfomycin resistance protein (FosA) catalyzes the Mn(II)- and K+-dependent addition of glutathione to the oxirane of the antibiotic fosfomycin. The crystal structure of FosA from Pseudomonas aeruginosa was solved at a resolution of 1.19 A by multiwavelength anomalous diffraction at the L-III edge of a Tl+ derivative. The structure solution took advantage of the ability of Tl+ to substitute for K+. The existence of multiple Tl sites in the asymmetric unit suggests that this may be a generally useful technique for phasing protein crystal structures. A 1.35 A resolution structure with phosphate bound in the active site shows that the Mn(II) center has a rare four-coordinate geometry. The structure of the fosfomycin complex at 1.19 A resolution indicates that the Mn(II) center is close to five-coordinate with trigonal bipyramidal geometry and a ligand set consisting of two histidines (H7 and H64) and one phosphonate oxygen occupying the equatorial sites and the carboxylate of E110 at one of the apical sites. The oxirane oxygen of the substrate is located at the other apical site but is 0.2 A beyond the average Mn-O distance for five-coordinate Mn(II). The Mn(II) center is proposed to stabilize the alkoxide in the transition state, while the nearby hydroxyl group of T9 acts as a proton donor in the reaction. The K+ ion located 6.5 A from the Mn(II) appears to help orient the substrate for nucleophilic attack.
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<StructureSection load='1lqp' size='340' side='right'caption='[[1lqp]], [[Resolution|resolution]] 1.19&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1lqp]] is a 2 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=1LQP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LQP FirstGlance]. <br>
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1LQP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa] with <scene name='pdbligand=K:'>K</scene>, <scene name='pdbligand=MN:'>MN</scene> and <scene name='pdbligand=FCN:'>FCN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LQP OCA].
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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]] 1.19&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FCN:FOSFOMYCIN'>FCN</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
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==Reference==
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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=1lqp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lqp OCA], [https://pdbe.org/1lqp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lqp RCSB], [https://www.ebi.ac.uk/pdbsum/1lqp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lqp ProSAT]</span></td></tr>
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Crystal structure of a genomically encoded fosfomycin resistance protein (FosA) at 1.19 A resolution by MAD phasing off the L-III edge of Tl(+)., Rife CL, Pharris RE, Newcomer ME, Armstrong RN, J Am Chem Soc. 2002 Sep 18;124(37):11001-3. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12224946 12224946]
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</table>
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[[Category: Glutathione transferase]]
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== Function ==
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[https://www.uniprot.org/uniprot/FOSA_PSEAE FOSA_PSEAE] Metalloglutathione transferase which confers resistance to fosfomycin by catalyzing the addition of glutathione to fosfomycin.
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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/lq/1lqp_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=1lqp ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Pseudomonas aeruginosa]]
[[Category: Pseudomonas aeruginosa]]
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[[Category: Single protein]]
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[[Category: Armstrong RN]]
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[[Category: Armstrong, R N.]]
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[[Category: Newcomer ME]]
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[[Category: Newcomer, M E.]]
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[[Category: Pharris RE]]
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[[Category: Pharris, R E.]]
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[[Category: Rife CL]]
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[[Category: Rife, C L.]]
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[[Category: FCN]]
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[[Category: K]]
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[[Category: MN]]
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[[Category: manganese binding]]
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[[Category: potassium binding loop]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:47:28 2008''
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Current revision

CRYSTAL STRUCTURE OF THE FOSFOMYCIN RESISTANCE PROTEIN (FOSA) CONTAINING BOUND SUBSTRATE

PDB ID 1lqp

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