1h72
From Proteopedia
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==About this Structure== | ==About this Structure== | ||
| - | 1H72 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/ | + | 1H72 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 HSE, ANP and TRS 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, HSE and TRS. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H72 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 10:28:39 2007'' |
Revision as of 08:23, 30 October 2007
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CRYSTAL STRUCTURE OF HOMOSERINE KINASE COMPLEXED WITH HSE
Overview
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 Structure
1H72 is a [Single protein] structure of sequence from [Methanocaldococcus jannaschii] with HSE, ANP and TRS as [ligands]. Active as [Homoserine kinase], with EC number [2.7.1.39]. Structure known Active Sites: ANP, HSE and TRS. Full crystallographic information is available from [OCA].
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:11535056
Page seeded by OCA on Tue Oct 30 10:28:39 2007
