1kkb
From Proteopedia
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| - | [[Image:1kkb.gif|left|200px]] | + | [[Image:1kkb.gif|left|200px]] |
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| - | '''Complex of Escherichia coli Adenylosuccinate Synthetase with IMP and Hadacidin''' | + | {{Structure |
| + | |PDB= 1kkb |SIZE=350|CAPTION= <scene name='initialview01'>1kkb</scene>, resolution 2.6Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=HAD:(CARBOXYHYDROXYAMINO)ETHANOIC+ACID'>HAD</scene> and <scene name='pdbligand=IMP:INOSINIC ACID'>IMP</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Adenylosuccinate_synthase Adenylosuccinate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.4.4 6.3.4.4] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Complex of Escherichia coli Adenylosuccinate Synthetase with IMP and Hadacidin''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1KKB is a [ | + | 1KKB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KKB OCA]. |
==Reference== | ==Reference== | ||
| - | IMP Alone Organizes the Active Site of Adenylosuccinate Synthetase from Escherichia coli., Hou Z, Wang W, Fromm HJ, Honzatko RB, J Biol Chem. 2002 Feb 22;277(8):5970-6. Epub 2001 Dec 12. PMID:[http:// | + | IMP Alone Organizes the Active Site of Adenylosuccinate Synthetase from Escherichia coli., Hou Z, Wang W, Fromm HJ, Honzatko RB, J Biol Chem. 2002 Feb 22;277(8):5970-6. Epub 2001 Dec 12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11741996 11741996] |
[[Category: Adenylosuccinate synthase]] | [[Category: Adenylosuccinate synthase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
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[[Category: IMP]] | [[Category: IMP]] | ||
[[Category: biosynthesis]] | [[Category: biosynthesis]] | ||
| - | [[Category: gtp-hydrolysing | + | [[Category: gtp-hydrolysing enzyme]] |
[[Category: induced fit]] | [[Category: induced fit]] | ||
[[Category: ligase]] | [[Category: ligase]] | ||
[[Category: purine nucleotide]] | [[Category: purine nucleotide]] | ||
| - | ''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 12:18:35 2008'' |
Revision as of 10:18, 20 March 2008
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| , resolution 2.6Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Activity: | Adenylosuccinate synthase, with EC number 6.3.4.4 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Complex of Escherichia coli Adenylosuccinate Synthetase with IMP and Hadacidin
Overview
A complete set of substrate/substrate analogs of adenylosuccinate synthetase from Escherichia coli induces dimer formation and a transition from a disordered to an ordered active site. The most striking of the ligand-induced effects is the movement of loop 40-53 by up to 9 A. Crystal structures of the partially ligated synthetase, which either combine IMP and hadacidin or IMP, hadacidin, and Mg(2+)-pyrophosphate, have ordered active sites, comparable with the fully ligated enzyme. More significantly, a crystal structure of the synthetase with IMP alone exhibits a largely ordered active site, which includes the 9 A movement of loop 40-53 but does not include conformational adjustments to backbone carbonyl 40 (Mg(2+) interaction element) and loop 298-304 (L-aspartate binding element). Interactions involving the 5'-phosphoryl group of IMP evidently trigger the formation of salt links some 30 A away. The above provides a structural basis for ligand binding synergism, effects on k(cat) due to mutations far from the site of catalysis, and the complete loss of substrate efficacy due to minor alterations of the 5'-phosphoryl group of IMP.
About this Structure
1KKB is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
IMP Alone Organizes the Active Site of Adenylosuccinate Synthetase from Escherichia coli., Hou Z, Wang W, Fromm HJ, Honzatko RB, J Biol Chem. 2002 Feb 22;277(8):5970-6. Epub 2001 Dec 12. PMID:11741996
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