2e20

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2e20.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2e20.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2e20| PDB=2e20 | SCENE= }}
{{STRUCTURE_2e20| PDB=2e20 | SCENE= }}
-
'''Crystal structure of Salmonella typhimurium propionate kinase (TdcD) in complex with diadenosine tetraphosphate (Ap4A)'''
+
===Crystal structure of Salmonella typhimurium propionate kinase (TdcD) in complex with diadenosine tetraphosphate (Ap4A)===
-
==Overview==
+
<!--
-
Recently, it has been shown that l-threonine can be catabolized non-oxidatively to propionate via 2-ketobutyrate. Propionate kinase (TdcD; EC 2.7.2.-) catalyses the last step of this metabolic process by enabling the conversion of propionyl phosphate and ADP to propionate and ATP. To provide insights into the substrate-binding pocket and catalytic mechanism of TdcD, the crystal structures of the enzyme from Salmonella typhimurium in complex with ADP and AMPPNP have been determined to resolutions of 2.2A and 2.3A, respectively, by molecular replacement using Methanosarcina thermophila acetate kinase (MAK; EC 2.7.2.1). Propionate kinase, like acetate kinase, contains a fold with the topology betabetabetaalphabetaalphabetaalpha, identical with that of glycerol kinase, hexokinase, heat shock cognaten 70 (Hsc70) and actin, the superfamily of phosphotransferases. The structure consists of two domains with the active site contained in a cleft at the domain interface. Examination of the active site pocket revealed a plausible structural rationale for the greater specificity of the enzyme towards propionate than acetate. This was further confirmed by kinetic studies with the purified enzyme, which showed about ten times lower K(m) for propionate (2.3 mM) than for acetate (26.9 mM). Comparison of TdcD complex structures with those of acetate and sugar kinase/Hsc70/actin obtained with different ligands has permitted the identification of catalytically essential residues involved in substrate binding and catalysis, and points to both structural and mechanistic similarities. In the well-characterized members of this superfamily, ATP phosphoryl transfer or hydrolysis is coupled to a large conformational change in which the two domains close around the active site cleft. The significant amino acid sequence similarity between TdcD and MAK has facilitated study of domain movement, which indicates that the conformation assumed by the two domains in the nucleotide-bound structure of TdcD may represent an intermediate point in the pathway of domain closure.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17894350}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17894350 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17894350}}
==About this Structure==
==About this Structure==
Line 19: Line 23:
==Reference==
==Reference==
 +
Crystal structures of Salmonella typhimurium propionate kinase and its complex with Ap4A: evidence for a novel Ap4A synthetic activity., Simanshu DK, Savithri HS, Murthy MR, Proteins. 2008 Mar;70(4):1379-88. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17894350 17894350]
 +
Crystal structures of ADP and AMPPNP-bound propionate kinase (TdcD) from Salmonella typhimurium: comparison with members of acetate and sugar kinase/heat shock cognate 70/actin superfamily., Simanshu DK, Savithri HS, Murthy MR, J Mol Biol. 2005 Sep 30;352(4):876-92. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16139298 16139298]
Crystal structures of ADP and AMPPNP-bound propionate kinase (TdcD) from Salmonella typhimurium: comparison with members of acetate and sugar kinase/heat shock cognate 70/actin superfamily., Simanshu DK, Savithri HS, Murthy MR, J Mol Biol. 2005 Sep 30;352(4):876-92. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16139298 16139298]
 +
 +
Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of propionate kinase (TdcD) from Salmonella typhimurium., Simanshu DK, Murthy MR, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Jan 1;61(Pt, 1):52-5. Epub 2004 Oct 23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16508089 16508089]
[[Category: Propionate kinase]]
[[Category: Propionate kinase]]
[[Category: Salmonella typhimurium]]
[[Category: Salmonella typhimurium]]
Line 36: Line 44:
[[Category: Tdcd]]
[[Category: Tdcd]]
[[Category: Transferase]]
[[Category: Transferase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 01:46:31 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Nov 5 10:41:13 2008''

Revision as of 08:41, 5 November 2008

Image:2e20.png

Template:STRUCTURE 2e20

Crystal structure of Salmonella typhimurium propionate kinase (TdcD) in complex with diadenosine tetraphosphate (Ap4A)

Template:ABSTRACT PUBMED 17894350

About this Structure

2E20 is a Single protein structure of sequence from Salmonella typhimurium. Full crystallographic information is available from OCA.

Reference

Crystal structures of Salmonella typhimurium propionate kinase and its complex with Ap4A: evidence for a novel Ap4A synthetic activity., Simanshu DK, Savithri HS, Murthy MR, Proteins. 2008 Mar;70(4):1379-88. PMID:17894350

Crystal structures of ADP and AMPPNP-bound propionate kinase (TdcD) from Salmonella typhimurium: comparison with members of acetate and sugar kinase/heat shock cognate 70/actin superfamily., Simanshu DK, Savithri HS, Murthy MR, J Mol Biol. 2005 Sep 30;352(4):876-92. PMID:16139298

Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of propionate kinase (TdcD) from Salmonella typhimurium., Simanshu DK, Murthy MR, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Jan 1;61(Pt, 1):52-5. Epub 2004 Oct 23. PMID:16508089

Page seeded by OCA on Wed Nov 5 10:41:13 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2e20"
Personal tools