1r0l: Difference between revisions

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[[Image:1r0l.jpg|left|200px]]
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{{STRUCTURE_1r0l|  PDB=1r0l  |  SCENE=  }}
'''1-deoxy-D-xylulose 5-phosphate reductoisomerase from zymomonas mobilis in complex with NADPH'''


==1-deoxy-D-xylulose 5-phosphate reductoisomerase from zymomonas mobilis in complex with NADPH==
<StructureSection load='1r0l' size='340' side='right'caption='[[1r0l]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1r0l]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Zymomonas_mobilis Zymomonas mobilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R0L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1R0L FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene></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=1r0l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r0l OCA], [https://pdbe.org/1r0l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1r0l RCSB], [https://www.ebi.ac.uk/pdbsum/1r0l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1r0l ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/DXR_ZYMMO DXR_ZYMMO] Catalyzes the NADP-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/r0/1r0l_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1r0l ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
1-Deoxy-d-xylulose-5-phosphate reductoisomerase (DXR) is the second enzyme in the non-mevalonate pathway of isoprenoid biosynthesis. The structure of the apo-form of this enzyme from Zymomonas mobilis has been solved and refined to 1.9-A resolution, and that of a binary complex with the co-substrate NADPH to 2.7-A resolution. The subunit of DXR consists of three domains. Residues 1-150 form the NADPH binding domain, which is a variant of the typical dinucleotide-binding fold. The second domain comprises a four-stranded mixed beta-sheet, with three helices flanking the sheet. Most of the putative active site residues are located on this domain. The C-terminal domain (residues 300-386) folds into a four-helix bundle. In solution and in the crystal, the enzyme forms a homo-dimer. The interface between the two monomers is formed predominantly by extension of the sheet in the second domain. The adenosine phosphate moiety of NADPH binds to the nucleotide-binding fold in the canonical way. The adenine ring interacts with the loop after beta1 and with the loops between alpha2 and beta2 and alpha5 and beta5. The nicotinamide ring is disordered in crystals of this binary complex. Comparisons to Escherichia coli DXR show that the two enzymes are very similar in structure, and that the active site architecture is highly conserved. However, there are differences in the recognition of the adenine ring of NADPH in the two enzymes.


==Overview==
Crystal structure of 1-deoxy-d-xylulose-5-phosphate reductoisomerase from Zymomonas mobilis at 1.9-A resolution.,Ricagno S, Grolle S, Bringer-Meyer S, Sahm H, Lindqvist Y, Schneider G Biochim Biophys Acta. 2004 Apr 8;1698(1):37-44. PMID:15063313<ref>PMID:15063313</ref>
1-Deoxy-d-xylulose-5-phosphate reductoisomerase (DXR) is the second enzyme in the non-mevalonate pathway of isoprenoid biosynthesis. The structure of the apo-form of this enzyme from Zymomonas mobilis has been solved and refined to 1.9-A resolution, and that of a binary complex with the co-substrate NADPH to 2.7-A resolution. The subunit of DXR consists of three domains. Residues 1-150 form the NADPH binding domain, which is a variant of the typical dinucleotide-binding fold. The second domain comprises a four-stranded mixed beta-sheet, with three helices flanking the sheet. Most of the putative active site residues are located on this domain. The C-terminal domain (residues 300-386) folds into a four-helix bundle. In solution and in the crystal, the enzyme forms a homo-dimer. The interface between the two monomers is formed predominantly by extension of the sheet in the second domain. The adenosine phosphate moiety of NADPH binds to the nucleotide-binding fold in the canonical way. The adenine ring interacts with the loop after beta1 and with the loops between alpha2 and beta2 and alpha5 and beta5. The nicotinamide ring is disordered in crystals of this binary complex. Comparisons to Escherichia coli DXR show that the two enzymes are very similar in structure, and that the active site architecture is highly conserved. However, there are differences in the recognition of the adenine ring of NADPH in the two enzymes.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1R0L is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Zymomonas_mobilis Zymomonas mobilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R0L OCA].
</div>
<div class="pdbe-citations 1r0l" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Crystal structure of 1-deoxy-d-xylulose-5-phosphate reductoisomerase from Zymomonas mobilis at 1.9-A resolution., Ricagno S, Grolle S, Bringer-Meyer S, Sahm H, Lindqvist Y, Schneider G, Biochim Biophys Acta. 2004 Apr 8;1698(1):37-44. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15063313 15063313]
*[[DXP reductoisomerase 3D Structures|DXP reductoisomerase 3D Structures]]
[[Category: 1-deoxy-D-xylulose-5-phosphate reductoisomerase]]
== References ==
[[Category: Single protein]]
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Zymomonas mobilis]]
[[Category: Zymomonas mobilis]]
[[Category: Bringer-Meyer, S.]]
[[Category: Bringer-Meyer S]]
[[Category: Grolle, S.]]
[[Category: Grolle S]]
[[Category: Lindqvist, Y.]]
[[Category: Lindqvist Y]]
[[Category: Ricagno, S.]]
[[Category: Ricagno S]]
[[Category: Sahm, H.]]
[[Category: Sahm H]]
[[Category: Schneider, G.]]
[[Category: Schneider G]]
[[Category: Fosmidomycin]]
[[Category: Nadph complex]]
[[Category: Non-mevalonate pathway]]
[[Category: Reductoisomerase]]
[[Category: Zymomonas mobili]]
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Retrieved from "https://proteopedia.org/1r0l"