2rd5
From Proteopedia
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|PDB= 2rd5 |SIZE=350|CAPTION= <scene name='initialview01'>2rd5</scene>, resolution 2.51Å | |PDB= 2rd5 |SIZE=350|CAPTION= <scene name='initialview01'>2rd5</scene>, resolution 2.51Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ARG:ARGININE'>ARG</scene>, <scene name='pdbligand=ATP:ADENOSINE-5'-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NLG:N-ACETYL-L-GLUTAMATE'>NLG</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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|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]) | |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]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2o66|2O66]], [[2o67|2O67]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2rd5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rd5 OCA], [http://www.ebi.ac.uk/pdbsum/2rd5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2rd5 RCSB]</span> | ||
}} | }} | ||
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[[Category: Moorhead, G B.G.]] | [[Category: Moorhead, G B.G.]] | ||
[[Category: Ng, K K.S.]] | [[Category: Ng, K K.S.]] | ||
| - | [[Category: ADP]] | ||
| - | [[Category: ARG]] | ||
| - | [[Category: ATP]] | ||
| - | [[Category: MG]] | ||
| - | [[Category: NLG]] | ||
[[Category: kinase]] | [[Category: kinase]] | ||
[[Category: nitrogen metabolism]] | [[Category: nitrogen metabolism]] | ||
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[[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 Mon Mar 31 04:59:04 2008'' |
Revision as of 01:59, 31 March 2008
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| , resolution 2.51Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , , | ||||||
| Gene: | T8H10.160 (Arabidopsis thaliana), AT4g01900, T7B11.16 (Arabidopsis thaliana) | ||||||
| Activity: | Acetylglutamate kinase, with EC number 2.7.2.8 | ||||||
| Related: | 2O66, 2O67
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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
Page seeded by OCA on Mon Mar 31 04:59:04 2008
