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3upy

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==Crystal structure of the Brucella abortus enzyme catalyzing the first committed step of the methylerythritol 4-phosphate pathway.==
==Crystal structure of the Brucella abortus enzyme catalyzing the first committed step of the methylerythritol 4-phosphate pathway.==
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<StructureSection load='3upy' size='340' side='right' caption='[[3upy]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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<StructureSection load='3upy' size='340' side='right'caption='[[3upy]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3upy]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Brucella_melitensis_biovar_abortus_2308 Brucella melitensis biovar abortus 2308]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UPY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3UPY FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3upy]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Brucella_abortus_2308 Brucella abortus 2308]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UPY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UPY FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FOM:3-[FORMYL(HYDROXY)AMINO]PROPYLPHOSPHONIC+ACID'>FOM</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene><br>
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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]] 1.8&#8491;</td></tr>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3upl|3upl]]</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=FOM:3-[FORMYL(HYDROXY)AMINO]PROPYLPHOSPHONIC+ACID'>FOM</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BAB2_0264, DRL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=359391 Brucella melitensis biovar Abortus 2308])</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=3upy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3upy OCA], [https://pdbe.org/3upy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3upy RCSB], [https://www.ebi.ac.uk/pdbsum/3upy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3upy ProSAT]</span></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3upy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3upy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3upy RCSB], [http://www.ebi.ac.uk/pdbsum/3upy PDBsum]</span></td></tr>
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</table>
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<table>
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== Function ==
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<div style="background-color:#fffaf0;">
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[https://www.uniprot.org/uniprot/Q2YIM3_BRUA2 Q2YIM3_BRUA2]
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== Publication Abstract from PubMed ==
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Most bacteria use the 2-C-methyl-D-erythritol 4-phosphate (MEP) pathway for the synthesis of their essential isoprenoid precursors. The absence of the MEP pathway in humans makes it a promising new target for the development of much needed new and safe antimicrobial drugs. However, bacteria show a remarkable metabolic plasticity for isoprenoid production. For example, the NADPH-dependent production of MEP from 1-deoxy-D-xylulose 5-phosphate in the first committed step of the MEP pathway is catalyzed by 1-deoxy-D-xylulose-5-phosphate reductoisomerase (DXR) in most bacteria, whereas an unrelated DXR-like (DRL) protein was recently found to catalyze the same reaction in some organisms, including the emerging human and animal pathogens Bartonella and Brucella. Here, we report the x-ray crystal structures of the Brucella abortus DRL enzyme in its apo form and in complex with the broad-spectrum antibiotic fosmidomycin solved to 1.5 and 1.8 A resolution, respectively. DRL is a dimer, with each polypeptide folding into three distinct domains starting with the NADPH-binding domain, in resemblance to the structure of bacterial DXR enzymes. Other than that, DRL and DXR show a low structural relationship, with a different disposition of the domains and a topologically unrelated C-terminal domain. In particular, the active site of DRL presents a unique arrangement, suggesting that the design of drugs that would selectively inhibit DRL-harboring pathogens without affecting beneficial or innocuous bacteria harboring DXR should be feasible. As a proof of concept, we identified two strong DXR inhibitors that have virtually no effect on DRL activity.
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Crystal structure of Brucella abortus deoxyxylulose-5-phosphate reductoisomerase-like (DRL) enzyme involved in isoprenoid biosynthesis.,Perez-Gil J, Calisto BM, Behrendt C, Kurz T, Fita I, Rodriguez-Concepcion M J Biol Chem. 2012 May 4;287(19):15803-9. Epub 2012 Mar 22. PMID:22442144<ref>PMID:22442144</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: Brucella melitensis biovar abortus 2308]]
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[[Category: Brucella abortus 2308]]
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[[Category: Calisto, B M.]]
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[[Category: Large Structures]]
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[[Category: Fita, I.]]
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[[Category: Calisto BM]]
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[[Category: Perez-Gil, J.]]
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[[Category: Fita I]]
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[[Category: Rodriguez-Concepcion, M]]
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[[Category: Perez-Gil J]]
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[[Category: Nadph binding]]
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[[Category: Rodriguez-Concepcion M]]
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[[Category: Oxidoreductase]]
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[[Category: Rossmann fold]]
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Current revision

Crystal structure of the Brucella abortus enzyme catalyzing the first committed step of the methylerythritol 4-phosphate pathway.

PDB ID 3upy

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