2rd5: Difference between revisions
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[[Image:2rd5.jpg|left|200px]]< | [[Image:2rd5.jpg|left|200px]] | ||
'''Structural basis for the regulation of N-acetylglutamate kinase by PII in Arabidopsis thaliana''' | {{Structure | ||
|PDB= 2rd5 |SIZE=350|CAPTION= <scene name='initialview01'>2rd5</scene>, resolution 2.51Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ARG:ARGININE'>ARG</scene>, <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=NLG:N-ACETYL-L-GLUTAMATE'>NLG</scene> and <scene name='pdbligand=ATP:ADENOSINE-5'-TRIPHOSPHATE'>ATP</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Acetylglutamate_kinase Acetylglutamate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.2.8 2.7.2.8] | |||
|GENE= T8H10.160 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 Arabidopsis thaliana]), AT4g01900, T7B11.16 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 Arabidopsis thaliana]) | |||
}} | |||
'''Structural basis for the regulation of N-acetylglutamate kinase by PII in Arabidopsis thaliana''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2RD5 is a [ | 2RD5 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RD5 OCA]. | ||
==Reference== | ==Reference== | ||
Structural basis for the regulation of N-acetylglutamate kinase by PII in Arabidopsis thaliana., Mizuno Y, Moorhead GB, Ng KK, J Biol Chem. 2007 Dec 7;282(49):35733-40. Epub 2007 Oct 3. PMID:[http:// | Structural basis for the regulation of N-acetylglutamate kinase by PII in Arabidopsis thaliana., Mizuno Y, Moorhead GB, Ng KK, J Biol Chem. 2007 Dec 7;282(49):35733-40. Epub 2007 Oct 3. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17913711 17913711] | ||
[[Category: Acetylglutamate kinase]] | [[Category: Acetylglutamate kinase]] | ||
[[Category: Arabidopsis thaliana]] | [[Category: Arabidopsis thaliana]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:34:54 2008'' | ||
Revision as of 16:34, 20 March 2008
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| 2rd5, resolution 2.51Å | |||||||||||||
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| Ligands: | MG, ARG, ADP, NLG and ATP | ||||||||||||
| Gene: | T8H10.160 (Arabidopsis thaliana), AT4g01900, T7B11.16 (Arabidopsis thaliana) | ||||||||||||
| Activity: | Acetylglutamate kinase, with EC number 2.7.2.8 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Structural basis for the regulation of N-acetylglutamate kinase by PII in Arabidopsis thaliana
Overview
PII is a highly conserved regulatory protein found in organisms across the three domains of life. In cyanobacteria and plants, PII relieves the feedback inhibition of the rate-limiting step in arginine biosynthesis catalyzed by N-acetylglutamate kinase (NAGK). To understand the molecular structural basis of enzyme regulation by PII, we have determined a 2.5-A resolution crystal structure of a complex formed between two homotrimers of PII and a single hexamer of NAGK from Arabidopsis thaliana bound to the metabolites N-acetylglutamate, ADP, ATP, and arginine. In PII, the T-loop and Trp(22) at the start of the alpha1-helix, which are both adjacent to the ATP-binding site of PII, contact two beta-strands as well as the ends of two central helices (alphaE and alphaG) in NAGK, the opposing ends of which form major portions of the ATP and N-acetylglutamate substrate-binding sites. The binding of Mg(2+).ATP to PII stabilizes a conformation of the T-loop that favors interactions with both open and closed conformations of NAGK. Interactions between PII and NAGK appear to limit the degree of opening and closing of the active-site cleft in opposition to a domain-separating inhibitory effect exerted by arginine, thus explaining the stimulatory effect of PII on the kinetics of arginine-inhibited NAGK.
About this Structure
2RD5 is a Protein complex structure of sequences from Arabidopsis thaliana. Full crystallographic information is available from OCA.
Reference
Structural basis for the regulation of N-acetylglutamate kinase by PII in Arabidopsis thaliana., Mizuno Y, Moorhead GB, Ng KK, J Biol Chem. 2007 Dec 7;282(49):35733-40. Epub 2007 Oct 3. PMID:17913711
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