2dt9: Difference between revisions

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[[Image:2dt9.jpg|left|200px]]<br /><applet load="2dt9" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:2dt9.jpg|left|200px]]
caption="2dt9, resolution 2.15&Aring;" />
 
'''Crystal structure of the regulatory subunit of aspartate kinase from Thermus flavus'''<br />
{{Structure
|PDB= 2dt9 |SIZE=350|CAPTION= <scene name='initialview01'>2dt9</scene>, resolution 2.15&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene> and <scene name='pdbligand=THR:THREONINE'>THR</scene>
|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]
|GENE= askB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=274 Thermus thermophilus])
}}
 
'''Crystal structure of the regulatory subunit of aspartate kinase from Thermus flavus'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
2DT9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with <scene name='pdbligand=ACT:'>ACT</scene> and <scene name='pdbligand=THR:'>THR</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DT9 OCA].  
2DT9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DT9 OCA].  


==Reference==
==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16232547 16232547]
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:[http://www.ncbi.nlm.nih.gov/pubmed/16232547 16232547]
[[Category: Aspartate kinase]]
[[Category: Aspartate kinase]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: regulatory subunit]]
[[Category: regulatory subunit]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:02:28 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:31:17 2008''

Revision as of 17:31, 20 March 2008

File:2dt9.jpg


PDB ID 2dt9

Drag the structure with the mouse to rotate
, resolution 2.15Å
Ligands: and
Gene: askB (Thermus thermophilus)
Activity: Aspartate kinase, with EC number 2.7.2.4
Coordinates: save as pdb, mmCIF, xml



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


OverviewOverview

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 StructureAbout this Structure

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

ReferenceReference

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

Page seeded by OCA on Thu Mar 20 16:31:17 2008

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