1auw: Difference between revisions

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[[Category: eye lens protein]]
[[Category: eye lens protein]]


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Revision as of 15:46, 30 October 2007

File:1auw.gif


1auw, resolution 2.5Å

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H91N DELTA 2 CRYSTALLIN FROM DUCK

OverviewOverview

The major soluble protein component of avian and reptilian eye lenses, delta crystallin, is highly homologous to the urea cycle enzyme, argininosuccinate lyase (ASL). In duck lenses there are two highly, homologous delta crystallins, termed delta I and delta II, that are 94%, identical in amino acid sequence. While delta II crystallin has been shown, to exhibit ASL activity in vitro, delta I crystallin is inactive. The, X-ray structure of a His to Asn mutant of duck delta II crystallin (H91N), has been determined to 2.5 A resolution using the molecular replacement, technique. The overall fold of the protein is similar to other members of, the superfamily to which this protein belongs, with the active site, located in a cleft between three different monomers of the tetrameric, protein. A ... [(full description)]

About this StructureAbout this Structure

1AUW is a [Single protein] structure of sequence from [Anas platyrhynchos]. Active as [Argininosuccinate lyase], with EC number [4.3.2.1]. Structure known Active Sites: CAA, CAB, CAC and CAD. Full crystallographic information is available from [OCA].

ReferenceReference

Structural comparison of the enzymatically active and inactive forms of delta crystallin and the role of histidine 91., Abu-Abed M, Turner MA, Vallee F, Simpson A, Slingsby C, Howell PL, Biochemistry. 1997 Nov 18;36(46):14012-22. PMID:9369472

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OCA