2gar
From Proteopedia
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m (Protected "2gar" [edit=sysop:move=sysop]) |
Revision as of 11:57, 7 January 2013
A PH-DEPENDENT STABLIZATION OF AN ACTIVE SITE LOOP OBSERVED FROM LOW AND HIGH PH CRYSTAL STRUCTURES OF MUTANT MONOMERIC GLYCINAMIDE RIBONUCLEOTIDE TRANSFORMYLASE
Template:ABSTRACT PUBMED 9698564
About this Structure
2gar is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
- Su Y, Yamashita MM, Greasley SE, Mullen CA, Shim JH, Jennings PA, Benkovic SJ, Wilson IA. A pH-dependent stabilization of an active site loop observed from low and high pH crystal structures of mutant monomeric glycinamide ribonucleotide transformylase at 1.8 to 1.9 A. J Mol Biol. 1998 Aug 21;281(3):485-99. PMID:9698564 doi:10.1006/jmbi.1998.1931
- Bhattacharyya R, Samanta U, Chakrabarti P. Aromatic-aromatic interactions in and around alpha-helices. Protein Eng. 2002 Feb;15(2):91-100. PMID:11917145
- Sandelin E. On hydrophobicity and conformational specificity in proteins. Biophys J. 2004 Jan;86(1 Pt 1):23-30. PMID:14695246 doi:10.1016/S0006-3495(04)74080-1
Categories: Escherichia coli | Phosphoribosylglycinamide formyltransferase | Benkovic, S J. | Greasley, S E. | Jennings, P A. | Mullen, C A. | Shim, J H. | Su, Y. | Wilson, I A. | Yamashita, M M. | Anti-cancer agent | Enzyme mechanism | Folate cofactor | Loop flexibility | Monomer-dimer association | Purine biosynthesis
