1auw

From Proteopedia
Revision as of 14:43, 30 October 2007 by OCA (talk | contribs)
Jump to navigation Jump to search
File:1auw.gif


1auw, resolution 2.5Å

Drag the structure with the mouse to rotate

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

Page seeded by OCA on Tue Oct 30 13:48:13 2007

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA