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1xrf

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[[Image:1xrf.gif|left|200px]]<br /><applet load="1xrf" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1xrf, resolution 1.65&Aring;" />
 
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'''The Crystal Structure of a Novel, Latent Dihydroorotase from Aquifex aeolicus at 1.7 A resolution'''<br />
 
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==Overview==
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==The Crystal Structure of a Novel, Latent Dihydroorotase from Aquifex aeolicus at 1.7 A resolution==
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Dihydroorotases (EC 3.5.2.3) catalyze the reversible cyclization of carbamoyl aspartate to form dihydroorotate in de novo pyrimidine biosynthesis. The X-ray structures of Aquifex aeolicus dihydroorotase in two space groups, C222(1) and C2, were determined at a resolution of 1.7A. These are the first structures of a type I dihydroorotase, a class of molecules that includes the dihydroorotase domain of mammalian CAD. The type I enzymes are more ancient and larger, at 45 kDa, than the type II enzymes exemplified by the 38 kDa Escherichia coli dihydroorotase. Both dihydroorotases are members of the metallo-dependent hydrolase superfamily, whose members have a distorted "TIM barrel" domain containing the active site. However, A.aeolicus dihydroorotase has a second, composite domain, which the E.coli enzyme lacks and has only one of the two zinc atoms present in the E.coli enzyme. A.aeolicus dihydroorotase is unique in exhibiting significant activity only when complexed with aspartate transcarbamoylase, whereas the E.coli dihydroorotase and the CAD dihydroorotase domain are active as free proteins. The latency of A.aeolicus dihydroorotase can be related to two differences between its structure and that of E.coli dihydroorotase: (1) the monoclinic structure has a novel cysteine ligand to the zinc that blocks the active site and possibly functions as a "cysteine switch"; and (2) active site residues that bind the substrate in E.coli dihydroorotase are located in disordered loops in both crystal structures of A.aeolicus dihydroorotase and may function as a disorder-to-order "entropy switch".
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<StructureSection load='1xrf' size='340' side='right'caption='[[1xrf]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1xrf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XRF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XRF 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]] 1.65&#8491;</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=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=1xrf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xrf OCA], [https://pdbe.org/1xrf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xrf RCSB], [https://www.ebi.ac.uk/pdbsum/1xrf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xrf ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PYRC_AQUAE PYRC_AQUAE]
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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/xr/1xrf_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=1xrf 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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1XRF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Dihydroorotase Dihydroorotase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.3 3.5.2.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XRF OCA].
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*[[Dihydroorotase 3D structures|Dihydroorotase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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The crystal structure of a novel, latent dihydroorotase from Aquifex aeolicus at 1.7A resolution., Martin PD, Purcarea C, Zhang P, Vaishnav A, Sadecki S, Guy-Evans HI, Evans DR, Edwards BF, J Mol Biol. 2005 May 6;348(3):535-47. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15826652 15826652]
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[[Category: Aquifex aeolicus]]
[[Category: Aquifex aeolicus]]
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[[Category: Dihydroorotase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Edwards BF]]
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[[Category: Edwards, B F.]]
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[[Category: Evans DR]]
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[[Category: Evans, D R.]]
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[[Category: Guy-Evans HI]]
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[[Category: Guy-Evans, H I.]]
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[[Category: Martin PD]]
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[[Category: Martin, P D.]]
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[[Category: Purcarea C]]
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[[Category: Purcarea, C.]]
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[[Category: Sadecki S]]
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[[Category: Sadecki, S.]]
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[[Category: Vaishnav A]]
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[[Category: Vaishnav, A.]]
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[[Category: Zhang P]]
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[[Category: Zhang, P.]]
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[[Category: SO4]]
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[[Category: ZN]]
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[[Category: amidohydrolase]]
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[[Category: dihydroorotase]]
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[[Category: metalloenzyme]]
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[[Category: pyrimidine]]
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[[Category: zinc]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:57:51 2008''
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Current revision

The Crystal Structure of a Novel, Latent Dihydroorotase from Aquifex aeolicus at 1.7 A resolution

PDB ID 1xrf

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