1scu

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1scu.gif|left|200px]]<br /><applet load="1scu" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1scu.gif|left|200px]]
-
caption="1scu, resolution 2.5&Aring;" />
+
 
-
'''THE CRYSTAL STRUCTURE OF SUCCINYL-COA SYNTHETASE FROM ESCHERICHIA COLI AT 2.5 ANGSTROMS RESOLUTION'''<br />
+
{{Structure
 +
|PDB= 1scu |SIZE=350|CAPTION= <scene name='initialview01'>1scu</scene>, resolution 2.5&Aring;
 +
|SITE=
 +
|LIGAND= <scene name='pdbligand=COA:COENZYME+A'>COA</scene> and <scene name='pdbligand=PHS:PHOSPHONIC ACID'>PHS</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=
 +
}}
 +
 
 +
'''THE CRYSTAL STRUCTURE OF SUCCINYL-COA SYNTHETASE FROM ESCHERICHIA COLI AT 2.5 ANGSTROMS RESOLUTION'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==About this Structure==
==About this Structure==
-
1SCU is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=COA:'>COA</scene> and <scene name='pdbligand=PHS:'>PHS</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SCU OCA].
+
1SCU 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=1SCU OCA].
==Reference==
==Reference==
-
The crystal structure of succinyl-CoA synthetase from Escherichia coli at 2.5-A resolution., Wolodko WT, Fraser ME, James MN, Bridger WA, J Biol Chem. 1994 Apr 8;269(14):10883-90. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8144675 8144675]
+
The crystal structure of succinyl-CoA synthetase from Escherichia coli at 2.5-A resolution., Wolodko WT, Fraser ME, James MN, Bridger WA, J Biol Chem. 1994 Apr 8;269(14):10883-90. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8144675 8144675]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Protein complex]]
[[Category: Protein complex]]
Line 22: Line 31:
[[Category: ligase (atp-binding)]]
[[Category: ligase (atp-binding)]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:00:11 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:03:16 2008''

Revision as of 12:03, 20 March 2008


PDB ID 1scu

Drag the structure with the mouse to rotate
, resolution 2.5Å
Ligands: and
Activity: Succinate--CoA ligase (ADP-forming), with EC number 6.2.1.5
Coordinates: save as pdb, mmCIF, xml



THE CRYSTAL STRUCTURE OF SUCCINYL-COA SYNTHETASE FROM ESCHERICHIA COLI AT 2.5 ANGSTROMS RESOLUTION


Overview

The x-ray crystal structure of succinyl-CoA synthetase (SCS) from Escherichia coli has been determined by the method of multiple isomorphous replacement to a resolution of 2.5 A. Crystals of SCS are tetragonal with a space group of P4(3)22 and unit cell dimensions of a = b = 98.47 A and c = 400.6 A. One molecule of SCS (142 kDa) is contained in the asymmetric unit. The current model has been refined to a conventional R factor of 21.6% with root mean square deviations from ideal stereochemistry of 0.022 A for bond lengths and 3.25 degrees for bond angles. The quaternary organization of the E. coli enzyme is an alpha 2 beta 2 heterotetramer. In this tetramer, the alpha-subunits interact only with the beta-subunits, whereas the beta-subunits interact to form the dimer of alpha beta-dimers. The two active site pockets are located at regions of contact between alpha- and beta-subunits. One molecule of coenzyme A is bound to each alpha-subunit at a typical nucleotide-binding motif, and His-246 of each alpha-subunit is phosphorylated. This phosphohistidine, a catalytic intermediate, is stabilized by two helix dipoles (the "power" helices), one from each of the two subunit types. A short segment of the beta-subunit from one alpha beta-dimer is in close proximity to the CoA-binding site of the other alpha beta-dimer, providing a possible rationale for the overall tetrameric structure.

About this Structure

1SCU is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.

Reference

The crystal structure of succinyl-CoA synthetase from Escherichia coli at 2.5-A resolution., Wolodko WT, Fraser ME, James MN, Bridger WA, J Biol Chem. 1994 Apr 8;269(14):10883-90. PMID:8144675

Page seeded by OCA on Thu Mar 20 14:03:16 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools