1tuu

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1tuu.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1tuu.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1tuu| PDB=1tuu | SCENE= }}
{{STRUCTURE_1tuu| PDB=1tuu | SCENE= }}
-
'''Acetate Kinase crystallized with ATPgS'''
+
===Acetate Kinase crystallized with ATPgS===
-
==Overview==
+
<!--
-
Acetate kinase catalyzes transfer of the gamma-phosphate of ATP to acetate. The only crystal structure reported for acetate kinase is the homodimeric enzyme from Methanosarcina thermophila containing ADP and sulfate in the active site (Buss, K. A., Cooper, D. C., Ingram-Smith, C., Ferry, J. G., Sanders, D. A., and Hasson, M. S. (2001) J. Bacteriol. 193, 680-686). Here we report two new crystal structure of the M. thermophila enzyme in the presence of substrate and transition state analogs. The enzyme co-crystallized with the ATP analog adenosine 5'-[gamma-thio]triphosphate contained AMP adjacent to thiopyrophosphate in the active site cleft of monomer B. The enzyme co-crystallized with ADP, acetate, Al(3+), and F(-) contained a linear array of ADP-AlF(3)-acetate in the active site cleft of monomer B. Together, the structures clarify the substrate binding sites and support a direct in-line transfer mechanism in which AlF(3) mimics the meta-phosphate transition state. Monomers A of both structures contained ADP and sulfate, and the active site clefts were closed less than in monomers B, suggesting that domain movement contributes to catalysis. The finding that His(180) was in close proximity to AlF(3) is consistent with a role for stabilization of the meta-phosphate that is in agreement with a previous report indicating that this residue is essential for catalysis. Residue Arg(241) was also found adjacent to AlF(3), consistent with a role for stabilization of the transition state. Kinetic analyses of Arg(241) and Arg(91) replacement variants indicated that these residues are essential for catalysis and also indicated a role in binding acetate.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15647264}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15647264 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15647264}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Alpha/beta]]
[[Category: Alpha/beta]]
[[Category: Two similar domain]]
[[Category: Two similar domain]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:23:46 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 11:49:13 2008''

Revision as of 08:49, 29 July 2008

Image:1tuu.png


PDB ID 1tuu

Drag the structure with the mouse to rotate
1tuu, resolution 2.50Å ()
Ligands: , , , ,
Gene: ACKA, ACK (Methanosarcina thermophila)
Activity: Acetate kinase, with EC number 2.7.2.1
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml



Acetate Kinase crystallized with ATPgS

Template:ABSTRACT PUBMED 15647264

About this Structure

1TUU is a Single protein structure of sequence from Methanosarcina thermophila. Full crystallographic information is available from OCA.

Reference

Structural and kinetic analyses of arginine residues in the active site of the acetate kinase from Methanosarcina thermophila., Gorrell A, Lawrence SH, Ferry JG, J Biol Chem. 2005 Mar 18;280(11):10731-42. Epub 2005 Jan 12. PMID:15647264

Page seeded by OCA on Tue Jul 29 11:49:13 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1tuu"
Personal tools