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1k5h

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(New page: 200px<br /><applet load="1k5h" size="450" color="white" frame="true" align="right" spinBox="true" caption="1k5h, resolution 2.50&Aring;" /> '''1-deoxy-D-xylulose-5...)
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[[Image:1k5h.jpg|left|200px]]<br /><applet load="1k5h" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1k5h, resolution 2.50&Aring;" />
 
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'''1-deoxy-D-xylulose-5-phosphate reductoisomerase'''<br />
 
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==Overview==
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==1-deoxy-D-xylulose-5-phosphate reductoisomerase==
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We have solved the 2.5-A crystal structure of, 1-deoxy-D-xylulose-5-phosphate reductoisomerase, an enzyme involved in the, mevalonate-independent 2-C-methyl-D-erythritol-4-phosphate pathway of, isoprenoid biosynthesis. The structure reveals that the enzyme is present, as a homodimer. Each monomer displays a V-like shape and is composed of an, amino-terminal dinucleotide binding domain, a connective domain, and a, carboxyl-terminal four-helix bundle domain. The connective domain is, responsible for dimerization and harbors most of the active site. The, strictly conserved acidic residues Asp(150), Glu(152), Glu(231), and, Glu(234) are clustered at the putative active site and are probably, involved in the binding of divalent cations mandatory for enzyme activity., The connective and four-helix bundle domains show significant mobility, upon superposition of the dinucleotide binding domains of the three, conformational states present in the asymmetric unit of the crystal. A, still more pronounced flexibility is observed for a loop spanning residues, 186 to 216, which adopts two completely different conformations within the, three protein conformers. A possible involvement of this loop in an, induced fit during substrate binding is discussed.
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<StructureSection load='1k5h' size='340' side='right'caption='[[1k5h]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1k5h]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K5H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1K5H FirstGlance]. <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]] 2.5&#8491;</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=1k5h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k5h OCA], [https://pdbe.org/1k5h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1k5h RCSB], [https://www.ebi.ac.uk/pdbsum/1k5h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1k5h ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/DXR_ECOLI DXR_ECOLI] Catalyzes the NADP-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).[HAMAP-Rule:MF_00183]
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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/k5/1k5h_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=1k5h ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1K5H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1K5H OCA].
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*[[DXP reductoisomerase 3D Structures|DXP reductoisomerase 3D Structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Crystal structure of 1-deoxy-D-xylulose-5-phosphate reductoisomerase, a crucial enzyme in the non-mevalonate pathway of isoprenoid biosynthesis., Reuter K, Sanderbrand S, Jomaa H, Wiesner J, Steinbrecher I, Beck E, Hintz M, Klebe G, Stubbs MT, J Biol Chem. 2002 Feb 15;277(7):5378-84. Epub 2001 Dec 7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11741911 11741911]
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[[Category: Escherichia coli K-12]]
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[[Category: Escherichia coli]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Beck E]]
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[[Category: Beck, E.]]
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[[Category: Hintz M]]
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[[Category: Hintz, M.]]
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[[Category: Jomaa H]]
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[[Category: Jomaa, H.]]
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[[Category: Klebe G]]
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[[Category: Klebe, G.]]
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[[Category: Reuter K]]
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[[Category: Reuter, K.]]
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[[Category: Sanderbrand S]]
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[[Category: Sanderbrand, S.]]
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[[Category: Steinbrecher I]]
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[[Category: Steinbrecher, I.]]
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[[Category: Stubbs MT]]
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[[Category: Stubbs, M.T.]]
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[[Category: Wiesner J]]
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[[Category: Wiesner, J.]]
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[[Category: alpha-helix]]
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[[Category: beta-barrel]]
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[[Category: dinucleotide binding motif]]
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[[Category: induced fit]]
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[[Category: variable loop]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:52:29 2007''
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Current revision

1-deoxy-D-xylulose-5-phosphate reductoisomerase

PDB ID 1k5h

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