1fb5

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[[Image:1fb5.jpg|left|200px]]<br /><applet load="1fb5" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1fb5, resolution 3.5&Aring;" />
 
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'''LOW RESOLUTION STRUCTURE OF OVINE ORNITHINE TRANSCARBMOYLASE IN THE UNLIGANDED STATE'''<br />
 
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==Overview==
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==LOW RESOLUTION STRUCTURE OF OVINE ORNITHINE TRANSCARBMOYLASE IN THE UNLIGANDED STATE==
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Ornithine transcarbamoylase from ovine liver has been purified to, homogeneity. Like all anabolic OTCs, the ovine enzyme is a trimer, constituted by identical subunits of 34 kDa. Sequence analysis of the 54, N-terminal residues of ovine OTC shows a high degree of homology with the, human enzyme. The optimum pH and the Michaelis constants for the catalytic, reaction were determined. The ovine enzyme is the most thermostable one, among mammals OTCs, its critical temperature being 6 degrees C higher than, those measured for the other enzymes. The enzyme has been crystallised and, the structure determined at 3.5 A resolution. Crystals belong to the cubic, P4(3)32 space group, with a = b = c = 184.7 A and a solvent content of, about 80%. There is no evidence of any ligand in the active site cavity, indicating that the crystals contain an unliganded or T state of the, enzyme. The unliganded OTCase enzyme adopts a trimeric structure which, in, the crystal, presents a three-fold axis coincident with the, crystallographic one. The conformation of each monomer in the trimer is, quite similar to that of the liganded human protein, with the exception of, a few loops, directly interacting with the substrate(s), which are able to, induce a rearrangement of the quaternary organisation of the trimer, that, accounts for the cooperative behaviour of the enzyme following the binding, of the substrates.
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<StructureSection load='1fb5' size='340' side='right'caption='[[1fb5]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1fb5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ovis_aries Ovis aries]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FB5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FB5 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]] 3.5&#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=NVA:NORVALINE'>NVA</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=1fb5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fb5 OCA], [https://pdbe.org/1fb5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fb5 RCSB], [https://www.ebi.ac.uk/pdbsum/1fb5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fb5 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/OTC_SHEEP OTC_SHEEP] Catalyzes the second step of the urea cycle, the condensation of carbamoyl phosphate with L-ornithine to form L-citrulline (PubMed:14527149). The urea cycle ensures the detoxification of ammonia by converting it to urea for excretion (Probable).<ref>PMID:14527149</ref>
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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/fb/1fb5_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=1fb5 ConSurf].
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<div style="clear:both"></div>
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==Disease==
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==See Also==
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Known disease associated with this structure: Ornithine transcarbamylase deficiency OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=300461 300461]]
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*[[Ornithine carbamoyltransferase 3D structures|Ornithine carbamoyltransferase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1FB5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Ovis_aries Ovis aries] with <scene name='pdbligand=NVA:'>NVA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Ornithine_carbamoyltransferase Ornithine carbamoyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.3.3 2.1.3.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FB5 OCA].
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Large Structures]]
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Functional and structural characterization of ovine ornithine transcarbamoylase., De Gregorio A, Battistutta R, Arena N, Panzalorto M, Francescato P, Valentini G, Bruno G, Zanotti G, Org Biomol Chem. 2003 Sep 21;1(18):3178-85. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14527149 14527149]
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[[Category: Ornithine carbamoyltransferase]]
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[[Category: Ovis aries]]
[[Category: Ovis aries]]
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[[Category: Single protein]]
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[[Category: Battistutta R]]
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[[Category: Battistutta, R.]]
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[[Category: Bruno G]]
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[[Category: Bruno, G.]]
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[[Category: De Gregorio A]]
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[[Category: Francescato, P.]]
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[[Category: Francescato P]]
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[[Category: Gregorio, A.De.]]
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[[Category: Panzalorto M]]
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[[Category: Panzalorto, M.]]
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[[Category: Zanotti G]]
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[[Category: Zanotti, G.]]
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[[Category: NVA]]
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[[Category: cooperativity]]
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[[Category: ornithine]]
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[[Category: t-state]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:46:50 2008''
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Current revision

LOW RESOLUTION STRUCTURE OF OVINE ORNITHINE TRANSCARBMOYLASE IN THE UNLIGANDED STATE

PDB ID 1fb5

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