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2pyw

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[[Image:2pyw.jpg|left|200px]]
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{{STRUCTURE_2pyw| PDB=2pyw | SCENE= }}
{{STRUCTURE_2pyw| PDB=2pyw | SCENE= }}
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'''Structure of A. thaliana 5-methylthioribose kinase in complex with ADP and MTR'''
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===Structure of A. thaliana 5-methylthioribose kinase in complex with ADP and MTR===
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==Overview==
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BACKGROUND: Metabolic variations exist between the methionine salvage pathway of humans and a number of plants and microbial pathogens. 5-Methylthioribose (MTR) kinase is a key enzyme required for methionine salvage in plants and many bacteria. The absence of a mammalian homolog suggests that MTR kinase is a good target for the design of specific herbicides or antibiotics. RESULTS: The structure of Arabidopsis thaliana MTR kinase co-crystallized with ATPgammaS and MTR has been determined at 1.9 A resolution. The structure is similar to B. subtilis MTR kinase and has the same protein kinase fold observed in other evolutionarily related protein kinase-like phosphotransferases. The active site is comparable between the two enzymes with the DXE-motif coordinating the nucleotide-Mg, the D238 of the HGD catalytic loop polarizing the MTR O1 oxygen, and the RR-motif interacting with the substrate MTR. Unlike its bacterial homolog, however, the Gly-rich loop (G-loop) of A. thaliana MTR kinase has an extended conformation, which shields most of the active site from solvent, a feature that resembles eukaryotic protein kinases more than the bacterial enzyme. The G- and W-loops of A. thaliana and B. subtilis MTR kinase adopt different conformations despite high sequence similarity. The ATPgammaS analog was hydrolyzed during the co-crystallization procedure, resulting in ADP in the active site. This suggests that the A. thaliana enzyme, like its bacterial homolog, may have significant ATPase activity in the absence of MTR. CONCLUSION: The structure of A. thaliana MTR kinase provides a template for structure-based design of agrochemicals, particularly herbicides whose effectiveness could be regulated by nutrient levels. Features of the MTR binding site offer an opportunity for a simple organic salt of an MTR analog to specifically inhibit MTR kinase.
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(as it appears on PubMed at http://www.pubmed.gov), where 17961230 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17961230}}
==About this Structure==
==About this Structure==
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[[Category: Refolding]]
[[Category: Refolding]]
[[Category: Transferase]]
[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 14:02:26 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 23:19:39 2008''

Revision as of 20:19, 28 July 2008

Image:2pyw.png

Template:STRUCTURE 2pyw

Structure of A. thaliana 5-methylthioribose kinase in complex with ADP and MTR

Template:ABSTRACT PUBMED 17961230

About this Structure

2PYW is a Single protein structure of sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA.

Reference

Structure of Arabidopsis thaliana 5-methylthioribose kinase reveals a more occluded active site than its bacterial homolog., Ku SY, Cornell KA, Howell PL, BMC Struct Biol. 2007 Oct 25;7:70. PMID:17961230

Page seeded by OCA on Mon Jul 28 23:19:39 2008

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