1h73: Difference between revisions
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==About this Structure== | ==About this Structure== | ||
1H73 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/ | 1H73 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]] with THR and ANP as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Homoserine_kinase Homoserine kinase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.39 2.7.1.39]]. Structure known Active Sites: ANP and THR. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H73 OCA]]. | ||
==Reference== | ==Reference== | ||
Structural basis for the catalysis and substrate specificity of homoserine kinase., Krishna SS, Zhou T, Daugherty M, Osterman A, Zhang H, Biochemistry. 2001 Sep 11;40(36):10810-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11535056 11535056] | Structural basis for the catalysis and substrate specificity of homoserine kinase., Krishna SS, Zhou T, Daugherty M, Osterman A, Zhang H, Biochemistry. 2001 Sep 11;40(36):10810-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11535056 11535056] | ||
[[Category: | [[Category: Homoserine kinase]] | ||
[[Category: Methanocaldococcus jannaschii]] | |||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Daugherty, M.]] | [[Category: Daugherty, M.]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 10:29:40 2007'' | ||
Revision as of 11:24, 30 October 2007
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CRYSTAL STRUCTURE OF HOMOSERINE KINASE COMPLEXED WITH THREONINE
OverviewOverview
Homoserine kinase (HSK), the fourth enzyme in the aspartate pathway of, amino acid biosynthesis, catalyzes the phosphorylation of L-homoserine, (Hse) to L-homoserine phosphate, an intermediate in the production of, L-threonine, L-isoleucine, and in higher plants, L-methionine. The, high-resolution structures of Methanococcus jannaschii HSK ternary, complexes with its amino acid substrate and ATP analogues have been, determined by X-ray crystallography. These structures reveal the, structural determinants of the tight and highly specific binding of Hse, which is coupled with local conformational changes that enforce the, sequestration of the substrate. The delta-hydroxyl group of bound Hse is, only 3.4 A away from the gamma-phosphate of the bound nucleotide, poised, for the in-line attack ... [(full description)]
About this StructureAbout this Structure
1H73 is a [Single protein] structure of sequence from [Methanocaldococcus jannaschii] with THR and ANP as [ligands]. Active as [Homoserine kinase], with EC number [2.7.1.39]. Structure known Active Sites: ANP and THR. Full crystallographic information is available from [OCA].
ReferenceReference
Structural basis for the catalysis and substrate specificity of homoserine kinase., Krishna SS, Zhou T, Daugherty M, Osterman A, Zhang H, Biochemistry. 2001 Sep 11;40(36):10810-8. PMID:11535056
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