1eb4
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(New page: 200px<br /> <applet load="1eb4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1eb4, resolution 2.0Å" /> '''HISTIDINE AMMONIA-LY...)
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Revision as of 15:36, 29 October 2007
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HISTIDINE AMMONIA-LYASE (HAL) MUTANT F329A FROM PSEUDOMONAS PUTIDA
Overview
Histidine ammonia-lyase requires a 4-methylidene-imidazole-5-one group, (MIO) that is produced autocatalytically by a cyclization and dehydration, step in a 3-residue loop of the polypeptide. The crystal structures of, three mutants have been established. Two mutants were inactive and failed, to form MIO, but remained unchanged elsewhere. The third mutant showed, very low activity and formed MIO, although it differed from an MIO-less, mutant only by an additional 329-C(beta) atom. This atom forms one, constraint during MIO formation, the other being the strongly connected, Asp145. An exploration of the conformational space of the MIO-forming loop, showed that the cyclization is probably enforced by a mechanic compression, in a late stage of chain folding and is catalyzed by a ... [(full description)]
About this Structure
1EB4 is a [Single protein] structure of sequence from [Pseudomonas putida] with SO4 and GOL as [ligands]. Active as [[1]], with EC number [4.3.1.3]. Full crystallographic information is available from [OCA].
Reference
Autocatalytic peptide cyclization during chain folding of histidine ammonia-lyase., Baedeker M, Schulz GE, Structure. 2002 Jan;10(1):61-7. PMID:11796111
Page seeded by OCA on Mon Oct 29 17:40:59 2007
