1cqj
From Proteopedia
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| - | [[Image:1cqj.gif|left|200px]] | + | [[Image:1cqj.gif|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF DEPHOSPHORYLATED E. COLI SUCCINYL-COA SYNTHETASE''' | + | {{Structure |
| + | |PDB= 1cqj |SIZE=350|CAPTION= <scene name='initialview01'>1cqj</scene>, resolution 2.9Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> and <scene name='pdbligand=COA:COENZYME A'>COA</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Succinate--CoA_ligase_(ADP-forming) Succinate--CoA ligase (ADP-forming)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.2.1.5 6.2.1.5] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF DEPHOSPHORYLATED E. COLI SUCCINYL-COA SYNTHETASE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1CQJ is a [ | + | 1CQJ is a [[Protein complex]] structure of sequences 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=1CQJ OCA]. |
==Reference== | ==Reference== | ||
| - | ADP-binding site of Escherichia coli succinyl-CoA synthetase revealed by x-ray crystallography., Joyce MA, Fraser ME, James MN, Bridger WA, Wolodko WT, Biochemistry. 2000 Jan 11;39(1):17-25. PMID:[http:// | + | ADP-binding site of Escherichia coli succinyl-CoA synthetase revealed by x-ray crystallography., Joyce MA, Fraser ME, James MN, Bridger WA, Wolodko WT, Biochemistry. 2000 Jan 11;39(1):17-25. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10625475 10625475] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: rossmann fold]] | [[Category: rossmann fold]] | ||
| - | ''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 10:27:36 2008'' |
Revision as of 08:27, 20 March 2008
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| , resolution 2.9Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Activity: | Succinate--CoA ligase (ADP-forming), with EC number 6.2.1.5 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF DEPHOSPHORYLATED E. COLI SUCCINYL-COA SYNTHETASE
Overview
Succinyl-CoA synthetase (SCS) catalyzes the following reversible reaction via a phosphorylated histidine intermediate (His 246alpha): succinyl-CoA + P(i) + NDP <--> succinate + CoA + NTP (N denotes adenosine or guanosine). To determine the structure of the enzyme with nucleotide bound, crystals of phosphorylated Escherichia coli SCS were soaked in successive experiments adopting progressive strategies. In the first experiment, 1 mM ADP (>15 x K(d)) was added; Mg(2+) ions were omitted to preclude the formation of an insoluble precipitate with the phosphate and ammonium ions. X-ray crystallography revealed that the enzyme was dephosphorylated, but the nucleotide did not remain bound to the enzyme (R(working) = 17.2%, R(free) = 22.8% for data to 2.9 A resolution). Catalysis requires Mg(2+) ions; hence, the "true" nucleotide substrate is probably an ADP-Mg(2+) complex. In the successful experiment, the phosphate buffer was exchanged with MOPS, the concentration of sulfate ions was lowered, and the concentrations of ADP and Mg(2+) ions were increased to 10.5 and 50 mM, respectively. X-ray diffraction data revealed an ADP-Mg(2+) complex bound in the ATP-grasp fold of the N-terminal domain of each beta-subunit (R(working) = 19.1%, R(free) = 24.7% for data to 3.3 A resolution). We describe the specific interactions of the nucleotide-Mg(2+) complex with SCS, compare these results with those for other proteins containing the ATP-grasp fold, and present a hypothetical model of the histidine-containing loop in the "down" position where it can interact with the nucleotide approximately 35 A from where His 246alpha is seen in both phosphorylated and dephosphorylated SCS.
About this Structure
1CQJ is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.
Reference
ADP-binding site of Escherichia coli succinyl-CoA synthetase revealed by x-ray crystallography., Joyce MA, Fraser ME, James MN, Bridger WA, Wolodko WT, Biochemistry. 2000 Jan 11;39(1):17-25. PMID:10625475
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