1v2g: Difference between revisions

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==About this Structure==
==About this Structure==
1V2G is a [[Single protein]] structure of sequence 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=1V2G OCA].  
1V2G is a 1 chain structure of sequence 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=1V2G OCA].  


==Reference==
==Reference==
Substrate specificities of Escherichia coli thioesterase I/protease I/lysophospholipase L1 are governed by its switch loop movement., Lo YC, Lin SC, Shaw JF, Liaw YC, Biochemistry. 2005 Feb 15;44(6):1971-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15697222 15697222]
<ref group="xtra">PMID:15697222</ref><ref group="xtra">PMID:12842470</ref><references group="xtra"/>
 
Crystal structure of Escherichia coli thioesterase I/protease I/lysophospholipase L1: consensus sequence blocks constitute the catalytic center of SGNH-hydrolases through a conserved hydrogen bond network., Lo YC, Lin SC, Shaw JF, Liaw YC, J Mol Biol. 2003 Jul 11;330(3):539-51. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12842470 12842470]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Liaw, Y C.]]
[[Category: Liaw, Y C.]]
[[Category: Lin, S C.]]
[[Category: Lin, S C.]]
Line 33: Line 30:
[[Category: Sgnh-hydrolase fold]]
[[Category: Sgnh-hydrolase fold]]


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Revision as of 16:58, 16 February 2009

File:1v2g.png

Template:STRUCTURE 1v2g

The L109P mutant of E. coli Thioesterase I/Protease I/Lysophospholipase L1 (TAP) in complexed with octanoic acid

Template:ABSTRACT PUBMED 15697222

About this Structure

1V2G is a 1 chain structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

  1. Lo YC, Lin SC, Shaw JF, Liaw YC. Substrate specificities of Escherichia coli thioesterase I/protease I/lysophospholipase L1 are governed by its switch loop movement. Biochemistry. 2005 Feb 15;44(6):1971-9. PMID:15697222 doi:10.1021/bi048109x
  2. Lo YC, Lin SC, Shaw JF, Liaw YC. Crystal structure of Escherichia coli thioesterase I/protease I/lysophospholipase L1: consensus sequence blocks constitute the catalytic center of SGNH-hydrolases through a conserved hydrogen bond network. J Mol Biol. 2003 Jul 11;330(3):539-51. PMID:12842470

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