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[[Image:1h3m.jpg|left|200px]]
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{{STRUCTURE_1h3m|  PDB=1h3m  |  SCENE=  }}
'''STRUCTURE OF 4-DIPHOSPHOCYTIDYL-2C-METHYL-D-ERYTHRITOL SYNTHETASE'''


==Structure of 4-diphosphocytidyl-2C-methyl-D-erythritol synthetase==
<StructureSection load='1h3m' size='340' side='right'caption='[[1h3m]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1h3m]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_BL21(DE3) Escherichia coli BL21(DE3)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H3M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H3M 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]] 2.4&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=N2P:PENTANE-1,5-DIAMINE'>N2P</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=1h3m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h3m OCA], [https://pdbe.org/1h3m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h3m RCSB], [https://www.ebi.ac.uk/pdbsum/1h3m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h3m ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ISPD_ECOLI ISPD_ECOLI] Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).[HAMAP-Rule:MF_00108]
== 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/h3/1h3m_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=1h3m ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
2-C-Methyl-D-erythritol 4-phosphate cytidylyltransferase is an essential enzyme in the mevalonate-independent pathway of isoprenoid biosynthesis. The structure of a tetragonal crystal form has been solved by molecular replacement and refined to 2.4 A resolution. Structure and sequence comparisons suggest that the enzyme is a suitable target for a structure-based approach to the development of novel broad-spectrum antibiotics. However, the absence of ligands in the enzyme active site together with the moderate resolution of the structure indicates that this tetragonal crystal form is inferior to that of a previously reported highly ordered monoclinic form [Richard et al. (2001), Nature Struct. Biol. 8, 641-647].


==Overview==
Structure of a tetragonal crystal form of Escherichia coli 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase.,Kemp LE, Bond CS, Hunter WN Acta Crystallogr D Biol Crystallogr. 2003 Mar;59(Pt 3):607-10. Epub 2003, Feb 21. PMID:12595740<ref>PMID:12595740</ref>
2-C-Methyl-D-erythritol 4-phosphate cytidylyltransferase is an essential enzyme in the mevalonate-independent pathway of isoprenoid biosynthesis. The structure of a tetragonal crystal form has been solved by molecular replacement and refined to 2.4 A resolution. Structure and sequence comparisons suggest that the enzyme is a suitable target for a structure-based approach to the development of novel broad-spectrum antibiotics. However, the absence of ligands in the enzyme active site together with the moderate resolution of the structure indicates that this tetragonal crystal form is inferior to that of a previously reported highly ordered monoclinic form [Richard et al. (2001), Nature Struct. Biol. 8, 641-647].


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1H3M is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H3M OCA].
</div>
<div class="pdbe-citations 1h3m" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Structure of a tetragonal crystal form of Escherichia coli 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase., Kemp LE, Bond CS, Hunter WN, Acta Crystallogr D Biol Crystallogr. 2003 Mar;59(Pt 3):607-10. Epub 2003, Feb 21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12595740 12595740]
*[[MEP cytidylyltransferase 3D structures|MEP cytidylyltransferase 3D structures]]
[[Category: 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase]]
== References ==
[[Category: Escherichia coli]]
<references/>
[[Category: Single protein]]
__TOC__
[[Category: Bond, C S.]]
</StructureSection>
[[Category: Hunter, W N.]]
[[Category: Large Structures]]
[[Category: Kemp, L E.]]
[[Category: Bond CS]]
[[Category: Isoprenoid]]
[[Category: Hunter WN]]
[[Category: Synthetase]]
[[Category: Kemp LE]]
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Retrieved from "https://proteopedia.org/1h3m"