1fb5

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[[Image:1fb5.jpg|left|200px]]
 
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==LOW RESOLUTION STRUCTURE OF OVINE ORNITHINE TRANSCARBMOYLASE IN THE UNLIGANDED STATE==
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The line below this paragraph, containing "STRUCTURE_1fb5", creates the "Structure Box" on the page.
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<StructureSection load='1fb5' size='340' side='right'caption='[[1fb5]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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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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or leave the SCENE parameter empty for the default display.
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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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{{STRUCTURE_1fb5| PDB=1fb5 | SCENE= }}
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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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'''LOW RESOLUTION STRUCTURE OF OVINE ORNITHINE TRANSCARBMOYLASE IN THE UNLIGANDED STATE'''
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==See Also==
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*[[Ornithine carbamoyltransferase 3D structures|Ornithine carbamoyltransferase 3D structures]]
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== References ==
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==Overview==
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<references/>
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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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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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1FB5 is a [[Single protein]] structure of sequence from [http://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].
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==Reference==
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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://www.ncbi.nlm.nih.gov/pubmed/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: 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 May 2 16:07:18 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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