1h72: Difference between revisions
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|PDB= 1h72 |SIZE=350|CAPTION= <scene name='initialview01'>1h72</scene>, resolution 1.8Å | |PDB= 1h72 |SIZE=350|CAPTION= <scene name='initialview01'>1h72</scene>, resolution 1.8Å | ||
|SITE= <scene name='pdbsite=ANP:Anp+Binding+Site+For+Chain+C'>ANP</scene>, <scene name='pdbsite=HSE:Hse+Binding+Site+For+Chain+C'>HSE</scene> and <scene name='pdbsite=TRS:Trs+Binding+Site+For+Chain+C'>TRS</scene> | |SITE= <scene name='pdbsite=ANP:Anp+Binding+Site+For+Chain+C'>ANP</scene>, <scene name='pdbsite=HSE:Hse+Binding+Site+For+Chain+C'>HSE</scene> and <scene name='pdbsite=TRS:Trs+Binding+Site+For+Chain+C'>TRS</scene> | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=HSE:L-HOMOSERINE'>HSE</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene> | ||
|ACTIVITY= [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] | |ACTIVITY= <span class='plainlinks'>[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] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1h72 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h72 OCA], [http://www.ebi.ac.uk/pdbsum/1h72 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1h72 RCSB]</span> | |||
}} | }} | ||
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[[Category: Zhang, H.]] | [[Category: Zhang, H.]] | ||
[[Category: Zhou, T.]] | [[Category: Zhou, T.]] | ||
[[Category: kinase]] | [[Category: kinase]] | ||
[[Category: threonine biosynthesis]] | [[Category: threonine biosynthesis]] | ||
[[Category: transferase]] | [[Category: transferase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:59:04 2008'' | ||
Revision as of 20:59, 30 March 2008
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| , resolution 1.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , and | ||||||
| Ligands: | , , | ||||||
| Activity: | Homoserine kinase, with EC number 2.7.1.39 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF HOMOSERINE KINASE COMPLEXED WITH HSE
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 at the gamma-phosphorus. The bound nucleotides are flexible at the triphosphate tail. Nevertheless, a Mg(2+) was located in one of the complexes that binds between the beta- and gamma-phosphates of the nucleotide with good ligand geometry and is coordinated by the side chain of Glu130. No strong nucleophile (base) can be located near the phosphoryl acceptor hydroxyl group. Therefore, we propose that the catalytic mechanism of HSK does not involve a catalytic base for activating the phosphoryl acceptor hydroxyl but instead is mediated via a transition state stabilization mechanism.
About this StructureAbout this Structure
1H72 is a Single protein structure of sequence from Methanocaldococcus jannaschii. 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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