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2jj4

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|SITE= <scene name='pdbsite=AC1:Nlg+Binding+Site+For+Chain+A'>AC1</scene> and <scene name='pdbsite=AC2:Nlg+Binding+Site+For+Chain+B'>AC2</scene>
|SITE= <scene name='pdbsite=AC1:Nlg+Binding+Site+For+Chain+A'>AC1</scene> and <scene name='pdbsite=AC2:Nlg+Binding+Site+For+Chain+B'>AC2</scene>
|LIGAND= <scene name='pdbligand=NLG:N-ACETYL-L-GLUTAMATE'>NLG</scene>
|LIGAND= <scene name='pdbligand=NLG:N-ACETYL-L-GLUTAMATE'>NLG</scene>
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|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]
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|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=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=[[1qy7|1QY7]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2jj4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jj4 OCA], [http://www.ebi.ac.uk/pdbsum/2jj4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2jj4 RCSB]</span>
}}
}}
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[[Category: Marco-Marin, C.]]
[[Category: Marco-Marin, C.]]
[[Category: Rubio, V.]]
[[Category: Rubio, V.]]
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[[Category: NLG]]
 
[[Category: acetylglutamate]]
[[Category: acetylglutamate]]
[[Category: amino-acid biosynthesis]]
[[Category: amino-acid biosynthesis]]
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[[Category: trimer]]
[[Category: trimer]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:42:37 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:59:05 2008''

Revision as of 00:59, 31 March 2008

Image:2jj4.gif


PDB ID 2jj4

Drag the structure with the mouse to rotate
, resolution 3.46Å
Sites: and
Ligands:
Activity: Acetylglutamate kinase, with EC number 2.7.2.8
Related: 1QY7


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



THE COMPLEX OF PII AND ACETYLGLUTAMATE KINASE FROM SYNECHOCOCCUS ELONGATUS PCC7942


Overview

Photosynthetic organisms can store nitrogen by synthesizing arginine, and, therefore, feedback inhibition of arginine synthesis must be relieved in these organisms when nitrogen is abundant. This relief is accomplished by the binding of the PII signal transduction protein to acetylglutamate kinase (NAGK), the controlling enzyme of arginine synthesis. Here, we describe the crystal structure of the complex between NAGK and PII of Synechococcus elongatus, at 2.75-A resolution. We prove the physiological relevance of the observed interactions by site-directed mutagenesis and functional studies. The complex consists of two polar PII trimers sandwiching one ring-like hexameric NAGK (a trimer of dimers) with the threefold axes of these molecules aligned. The binding of PII favors a narrow ring conformation of the NAGK hexamer that is associated with arginine sites having low affinity for this inhibitor. Each PII subunit contacts one NAGK subunit only. The contacts map in the inner circumference of the NAGK ring and involve two surfaces of the PII subunit. One surface is on the PII body and interacts with the C-domain of the NAGK subunit, helping widen the arginine site found on the other side of this domain. The other surface is at the distal region of a protruding large loop (T-loop) that presents a novel compact shape. This loop is inserted in the interdomain crevice of the NAGK subunit, contacting mainly the N-domain, and playing key roles in anchoring PII on NAGK, in activating NAGK, and in complex formation regulation by MgATP, ADP, 2-oxoglutarate, and by phosphorylation of serine-49.

About this Structure

2JJ4 is a Protein complex structure of sequences from Synechococcus elongatus. Full crystallographic information is available from OCA.

Reference

The crystal structure of the complex of PII and acetylglutamate kinase reveals how PII controls the storage of nitrogen as arginine., Llacer JL, Contreras A, Forchhammer K, Marco-Marin C, Gil-Ortiz F, Maldonado R, Fita I, Rubio V, Proc Natl Acad Sci U S A. 2007 Nov 6;104(45):17644-9. Epub 2007 Oct 24. PMID:17959776

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