2o1c: Difference between revisions

Revision as of 16:11, 30 January 2013

2o1c is a 4 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA.

↑ Gabelli SB, Bianchet MA, Xu W, Dunn CA, Niu ZD, Amzel LM, Bessman MJ. Structure and function of the E. coli dihydroneopterin triphosphate pyrophosphatase: a Nudix enzyme involved in folate biosynthesis. Structure. 2007 Aug;15(8):1014-22. PMID:17698004 doi:S0969-2126(07)00252-3
↑ O'Handley SF, Frick DN, Bullions LC, Mildvan AS, Bessman MJ. Escherichia coli orf17 codes for a nucleoside triphosphate pyrophosphohydrolase member of the MutT family of proteins. Cloning, purification, and characterization of the enzyme. J Biol Chem. 1996 Oct 4;271(40):24649-54. PMID:8798731

@@ Line 1: / Line 1: @@
 [[Image:2o1c.png|left|200px]]
-<!--
-The line below this paragraph, containing "STRUCTURE_2o1c", creates the "Structure Box" on the page.
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-or leave the SCENE parameter empty for the default display.
--->
 {{STRUCTURE_2o1c|  PDB=2o1c  |  SCENE=  }}
 ===Structure of the E. coli dihydroneopterin triphosphate pyrophosphohydrolase===
-<!--
-The line below this paragraph, {{ABSTRACT_PUBMED_17698004}}, adds the Publication Abstract to the page
-(as it appears on PubMed at http://www.pubmed.gov), where 17698004 is the PubMed ID number.
--->
 {{ABSTRACT_PUBMED_17698004}}
@@ Line 22: / Line 11: @@
 ==Reference==
-<ref group="xtra">PMID:17698004</ref><ref group="xtra">PMID:8798731</ref><ref group="xtra">PMID:4362677</ref><references group="xtra"/>
+<ref group="xtra">PMID:017698004</ref><ref group="xtra">PMID:008798731</ref><references group="xtra"/>
 [[Category: Escherichia coli]]
 [[Category: Amzel, L M.]]
 [[Category: Bianchet, M A.]]
 [[Category: Gabelli, S B.]]
+[[Category: Hydrolase]]
 [[Category: Nudix ntp hydrolase ntp pyrophosphohydrolase mutt dihydroneopterin triphosphate pyrophosphohydrolase folate biosynthesis]]