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3qvh

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==Crystal structure of fosfomycin resistance kinase FomA from Streptomyces wedmorensis complexed with ADP==
==Crystal structure of fosfomycin resistance kinase FomA from Streptomyces wedmorensis complexed with ADP==
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<StructureSection load='3qvh' size='340' side='right' caption='[[3qvh]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
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<StructureSection load='3qvh' size='340' side='right'caption='[[3qvh]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3qvh]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptomyces_wedmorensis Streptomyces wedmorensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QVH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3QVH FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3qvh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_wedmorensis Streptomyces wedmorensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QVH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QVH FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></td></tr>
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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]] 1.85&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3qun|3qun]], [[3quo|3quo]], [[3qur|3qur]], [[3qvf|3qvf]], [[3d40|3d40]], [[3d41|3d41]]</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=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fomA, fosfomycin resistance kinase ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=43759 Streptomyces wedmorensis])</td></tr>
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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=3qvh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qvh OCA], [https://pdbe.org/3qvh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qvh RCSB], [https://www.ebi.ac.uk/pdbsum/3qvh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qvh ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3qvh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qvh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qvh RCSB], [http://www.ebi.ac.uk/pdbsum/3qvh PDBsum]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q56187_STRWE Q56187_STRWE]
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We present here the crystal structures of fosfomycin resistance protein (FomA) complexed with MgATP, with ATP and fosfomycin, with MgADP and fosfomycin vanadate, with MgADP and the product of the enzymatic reaction, fosfomycin monophosphate, and with ADP at 1.87, 1.58, 1.85, 1.57, and 1.85 A resolution, respectively. Structures of these complexes that approximate different reaction steps allowed us to distinguish the catalytically active conformation of ATP and to reconstruct the model of the MgATP.fosfomycin complex. According to the model, the triphosphate tail of the nucleotide is aligned toward the phosphonate moiety of fosfomycin, in contast to the previously published MgAMPPNP complex, with the attacking fosfomycin oxygen positioned 4 A from the gamma-phosphorus of ATP. Site-directed mutagenesis studies and comparison of these structures with that of homologous N-acetyl-l-glutamate and isopentenyl phosphate kinases allowed us to propose a model of phosphorylation of fosfomycin by FomA enzyme. A Mg cation ligates all three phosphate groups of ATP and together with positively charged K216, K9, K18, and H58 participates in the dissipation of negative charge during phosphoryl transfer, indicating that the transferred phosphate group is highly negatively charged, which would be expected for an associative mechanism. K216 polarizes the gamma-phosphoryl group of ATP. K9, K18, and H58 participate in stabilization of the transition state. D150 and D208 play organizational roles in catalysis. S148, S149, and T210 participate in fosfomycin binding, with T210 being crucial for catalysis. Hence, it appears that as in the homologous enzymes, FomA-catalyzed phosphoryl transfer takes place by an in-line predominantly associative mechanism.
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Structural and Biochemical Insights into the Mechanism of Fosfomycin Phosphorylation by Fosfomycin Resistance Kinase FomA.,Pakhomova S, Bartlett SG, Doerner PA, Newcomer ME Biochemistry. 2011 Jul 18. PMID:21728358<ref>PMID:21728358</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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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Large Structures]]
[[Category: Streptomyces wedmorensis]]
[[Category: Streptomyces wedmorensis]]
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[[Category: Bartlett, S G]]
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[[Category: Bartlett SG]]
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[[Category: Doerner, P A]]
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[[Category: Doerner PA]]
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[[Category: Newcomer, M E]]
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[[Category: Newcomer ME]]
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[[Category: Pakhomova, S]]
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[[Category: Pakhomova S]]
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[[Category: Antibiotic resistance]]
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[[Category: Fosfomycin]]
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[[Category: Kinase]]
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[[Category: Phosphoryl transfer]]
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[[Category: Transferase]]
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Current revision

Crystal structure of fosfomycin resistance kinase FomA from Streptomyces wedmorensis complexed with ADP

PDB ID 3qvh

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