1fb5
From Proteopedia
(New page: 200px<br /> <applet load="1fb5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fb5, resolution 3.5Å" /> '''LOW RESOLUTION STRUC...) |
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caption="1fb5, resolution 3.5Å" /> | caption="1fb5, resolution 3.5Å" /> | ||
'''LOW RESOLUTION STRUCTURE OF OVINE ORNITHINE TRANSCARBMOYLASE IN THE UNLIGANDED STATE'''<br /> | '''LOW RESOLUTION STRUCTURE OF OVINE ORNITHINE TRANSCARBMOYLASE IN THE UNLIGANDED STATE'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 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 NVA 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:// | + | 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]. |
==Reference== | ==Reference== | ||
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[[Category: t-state]] | [[Category: t-state]] | ||
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Revision as of 13:46, 15 February 2008
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LOW RESOLUTION STRUCTURE OF OVINE ORNITHINE TRANSCARBMOYLASE IN THE UNLIGANDED STATE
Contents |
Overview
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.
Disease
Known disease associated with this structure: Ornithine transcarbamylase deficiency OMIM:[300461]
About this Structure
1FB5 is a Single protein structure of sequence from Ovis aries with as ligand. Active as Ornithine carbamoyltransferase, with EC number 2.1.3.3 Full crystallographic information is available from OCA.
Reference
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:14527149
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