1rtr

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Current revision (08:25, 14 February 2024) (edit) (undo)
 
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<StructureSection load='1rtr' size='340' side='right'caption='[[1rtr]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
<StructureSection load='1rtr' size='340' side='right'caption='[[1rtr]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1rtr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"micrococcus_aureus"_(rosenbach_1884)_zopf_1885 "micrococcus aureus" (rosenbach 1884) zopf 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RTR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RTR FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1rtr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RTR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RTR FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1rqi|1rqi]], [[1rqj|1rqj]]</div></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]] 2.5&#8491;</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=1rtr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rtr OCA], [https://pdbe.org/1rtr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rtr RCSB], [https://www.ebi.ac.uk/pdbsum/1rtr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rtr ProSAT]</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=1rtr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rtr OCA], [https://pdbe.org/1rtr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rtr RCSB], [https://www.ebi.ac.uk/pdbsum/1rtr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rtr ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/A0A0H3JWH0_STAAW A0A0H3JWH0_STAAW]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=1rtr ConSurf].
</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=1rtr ConSurf].
<div style="clear:both"></div>
<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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Farnesyl pyrophosphate synthetase (FPPS) synthesizes farnesyl pyrophosphate through successive condensations of isopentyl pyrophosphate with dimethylallyl pyrophosphate and geranyl pyrophosphate. Nitrogen-containing bisphosphonate drugs used to treat osteoclast-mediated bone resorption and tumor-induced hypercalcemia are potent inhibitors of the enzyme. Here we present crystal structures of substrate and bisphosphonate complexes of FPPS. The structures reveal how enzyme conformational changes organize conserved active site residues to exploit metal-induced ionization and substrate positioning for catalysis. The structures further demonstrate how nitrogen-containing bisphosphonates mimic a carbocation intermediate to inhibit the enzyme. Together, these FPPS complexes provide a structural template for the design of novel inhibitors that may prove useful for the treatment of osteoporosis and other clinical indications including cancer.
 
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Structural basis for bisphosphonate-mediated inhibition of isoprenoid biosynthesis.,Hosfield DJ, Zhang Y, Dougan DR, Broun A, Tari LW, Swanson RV, Finn J J Biol Chem. 2004 Mar 5;279(10):8526-9. Epub 2003 Dec 12. PMID:14672944<ref>PMID:14672944</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 1rtr" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
*[[Farnesyl diphosphate synthase 3D structures|Farnesyl diphosphate synthase 3D structures]]
*[[Farnesyl diphosphate synthase 3D structures|Farnesyl diphosphate synthase 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Brooun, A]]
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[[Category: Staphylococcus aureus]]
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[[Category: Dougan, D R]]
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[[Category: Brooun A]]
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[[Category: Finn, J]]
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[[Category: Dougan DR]]
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[[Category: Hosfield, D J]]
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[[Category: Finn J]]
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[[Category: Swanson, R V]]
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[[Category: Hosfield DJ]]
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[[Category: Tari, L W]]
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[[Category: Swanson RV]]
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[[Category: Zhang, Y]]
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[[Category: Tari LW]]
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[[Category: Transferase]]
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[[Category: Zhang Y]]

Current revision

Crystal Structure of S. Aureus Farnesyl Pyrophosphate Synthase

PDB ID 1rtr

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