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1oat

From Proteopedia

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[[Image:1oat.png|left|200px]]
 
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{{STRUCTURE_1oat| PDB=1oat | SCENE= }}
{{STRUCTURE_1oat| PDB=1oat | SCENE= }}
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===ORNITHINE AMINOTRANSFERASE===
===ORNITHINE AMINOTRANSFERASE===
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{{ABSTRACT_PUBMED_9514741}}
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{{ABSTRACT_PUBMED_9514741}}
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==Disease==
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[[http://www.uniprot.org/uniprot/OAT_HUMAN OAT_HUMAN]] Defects in OAT are the cause of hyperornithinemia with gyrate atrophy of choroid and retina (HOGA) [MIM:[http://omim.org/entry/258870 258870]]. HOGA is a slowly progressive blinding autosomal recessive disorder.<ref>PMID:3375240</ref><ref>PMID:2793865</ref><ref>PMID:1612597</ref><ref>PMID:1737786</ref><ref>PMID:7887415</ref><ref>PMID:7668253</ref>
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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<ref group="xtra">PMID:009514741</ref><ref group="xtra">PMID:016754985</ref><references group="xtra"/>
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<ref group="xtra">PMID:009514741</ref><ref group="xtra">PMID:016754985</ref><references group="xtra"/><references/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Ornithine aminotransferase]]
[[Category: Ornithine aminotransferase]]

Revision as of 18:33, 24 March 2013

Template:STRUCTURE 1oat

Contents

ORNITHINE AMINOTRANSFERASE

Template:ABSTRACT PUBMED 9514741

Disease

[OAT_HUMAN] Defects in OAT are the cause of hyperornithinemia with gyrate atrophy of choroid and retina (HOGA) [MIM:258870]. HOGA is a slowly progressive blinding autosomal recessive disorder.[1][2][3][4][5][6]

About this Structure

1oat is a 3 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

  • Shen BW, Hennig M, Hohenester E, Jansonius JN, Schirmer T. Crystal structure of human recombinant ornithine aminotransferase. J Mol Biol. 1998 Mar 20;277(1):81-102. PMID:9514741 doi:10.1006/jmbi.1997.1583
  • Tripathi SM, Ramachandran R. Overexpression, purification and crystallization of lysine epsilon-aminotransferase (Rv3290c) from Mycobacterium tuberculosis H37Rv. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Jun 1;62(Pt, 6):572-5. Epub 2006 May 31. PMID:16754985 doi:10.1107/S1744309106016824
  1. ↑ Ramesh V, McClatchey AI, Ramesh N, Benoit LA, Berson EL, Shih VE, Gusella JF. Molecular basis of ornithine aminotransferase deficiency in B-6-responsive and -nonresponsive forms of gyrate atrophy. Proc Natl Acad Sci U S A. 1988 Jun;85(11):3777-80. PMID:3375240
  2. ↑ Inana G, Chambers C, Hotta Y, Inouye L, Filpula D, Pulford S, Shiono T. Point mutation affecting processing of the ornithine aminotransferase precursor protein in gyrate atrophy. J Biol Chem. 1989 Oct 15;264(29):17432-6. PMID:2793865
  3. ↑ Michaud J, Brody LC, Steel G, Fontaine G, Martin LS, Valle D, Mitchell G. Strand-separating conformational polymorphism analysis: efficacy of detection of point mutations in the human ornithine delta-aminotransferase gene. Genomics. 1992 Jun;13(2):389-94. PMID:1612597
  4. ↑ Brody LC, Mitchell GA, Obie C, Michaud J, Steel G, Fontaine G, Robert MF, Sipila I, Kaiser-Kupfer M, Valle D. Ornithine delta-aminotransferase mutations in gyrate atrophy. Allelic heterogeneity and functional consequences. J Biol Chem. 1992 Feb 15;267(5):3302-7. PMID:1737786
  5. ↑ Michaud J, Thompson GN, Brody LC, Steel G, Obie C, Fontaine G, Schappert K, Keith CG, Valle D, Mitchell GA. Pyridoxine-responsive gyrate atrophy of the choroid and retina: clinical and biochemical correlates of the mutation A226V. Am J Hum Genet. 1995 Mar;56(3):616-22. PMID:7887415
  6. ↑ Kobayashi T, Ogawa H, Kasahara M, Shiozawa Z, Matsuzawa T. A single amino acid substitution within the mature sequence of ornithine aminotransferase obstructs mitochondrial entry of the precursor. Am J Hum Genet. 1995 Aug;57(2):284-91. PMID:7668253

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