2dt9

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|PDB= 2dt9 |SIZE=350|CAPTION= <scene name='initialview01'>2dt9</scene>, resolution 2.15&Aring;
|PDB= 2dt9 |SIZE=350|CAPTION= <scene name='initialview01'>2dt9</scene>, resolution 2.15&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene> and <scene name='pdbligand=THR:THREONINE'>THR</scene>
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|LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=THR:THREONINE'>THR</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Aspartate_kinase Aspartate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.2.4 2.7.2.4]
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Aspartate_kinase Aspartate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.2.4 2.7.2.4] </span>
|GENE= askB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=274 Thermus thermophilus])
|GENE= askB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=274 Thermus thermophilus])
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|DOMAIN=
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|RELATEDENTRY=[[2dtj|2DTJ]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2dt9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dt9 OCA], [http://www.ebi.ac.uk/pdbsum/2dt9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2dt9 RCSB]</span>
}}
}}
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[[Category: Tomita, T.]]
[[Category: Tomita, T.]]
[[Category: Yoshida, A.]]
[[Category: Yoshida, A.]]
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[[Category: ACT]]
 
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[[Category: THR]]
 
[[Category: protein-ligand complex]]
[[Category: protein-ligand complex]]
[[Category: regulatory subunit]]
[[Category: regulatory subunit]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:31:17 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:39:10 2008''

Revision as of 23:39, 30 March 2008


PDB ID 2dt9

Drag the structure with the mouse to rotate
, resolution 2.15Å
Ligands: ,
Gene: askB (Thermus thermophilus)
Activity: Aspartate kinase, with EC number 2.7.2.4
Related: 2DTJ


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Crystal structure of the regulatory subunit of aspartate kinase from Thermus flavus


Overview

To reveal the catalytic mechanism of Thermus aspartate kinase, each of 29 amino acid residues that were highly conserved in the sequenced aspartate kinases, was replaced with alanine or leucine by PCR site-directed mutagenesis. Comparison of the kinetic parameters of these mutants with those of the wild-type aspartate kinase suggested that Thr47 was involved in binding aspartate and that Lys7 and Glu74 were involved in catalysis. Analysis of the effective concentrations of magnesium ion on the activity showed that the mutants with replacements at Ser41, Thr47, Asp154 and Asp182 required higher concentrations of magnesium ion. This suggests that these four residues play important roles in the binding of magnesium ions which are required for enzymatic activity.

About this Structure

2DT9 is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.

Reference

Kinetic and mutation analyses of aspartate kinase from Thermus flavus., Kobashi N, Nishiyama M, Tanokura M, J Biosci Bioeng. 1999;87(6):739-45. PMID:16232547

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