1am7

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[[Category: transglycosylase]]
[[Category: transglycosylase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 11:52:57 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 14:49:44 2007''

Revision as of 12:45, 30 October 2007


1am7, resolution 2.3Å

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LYSOZYME FROM BACTERIOPHAGE LAMBDA

Overview

Like other lysozymes, the bacteriophage lambda lysozyme is involved in the, digestion of bacterial walls. This enzyme is remarkable in that its, mechanism of action is different from the classical lysozyme's mechanism., From the point of view of protein evolution, it shows features of, lysozymes from different classes. The crystal structure of the enzyme in, which all tryptophan residues have been replaced by aza-tryptophan has, been solved by X-ray crystallography at 2.3 A using a combination of, multiple isomorphous replacement, non-crystallographic symmetry averaging, and density modification techniques. There are three molecules in the, asymmetric unit. The characteristic structural elements of lysozymes are, conserved: each molecule is organized in two domains connected by a helix, ... [(full description)]

About this Structure

1AM7 is a [Single protein] structure of sequence from [Enterobacteria phage lambda] with IPA as [ligand]. Structure known Active Sites: CAA, CAB and CAC. Full crystallographic information is available from [OCA].

Reference

Crystal structure of the lysozyme from bacteriophage lambda and its relationship with V and C-type lysozymes., Evrard C, Fastrez J, Declercq JP, J Mol Biol. 1998 Feb 13;276(1):151-64. PMID:9514719

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