152l

From Proteopedia
Revision as of 11:20, 20 November 2007 by OCA (talk | contribs) (New page: left|200px<br /><applet load="152l" size="450" color="white" frame="true" align="right" spinBox="true" caption="152l, resolution 2.0Å" /> '''CONSERVATION OF SOLVE...)
(diff) ← Older revision | Latest revision (diff) | Newer revision → (diff)
Jump to navigation Jump to search
File:152l.jpg


152l, resolution 2.0Å

Drag the structure with the mouse to rotate

CONSERVATION OF SOLVENT-BINDING SITES IN 10 CRYSTAL FORMS OF T4 LYSOZYME

OverviewOverview

Solvent-binding sites were compared in 10 different crystal forms of phage, T4 lysozyme that were refined using data from 2.6 A to 1.7 A resolution., The sample included 18 crystallographically independent lysozyme, molecules. Despite different crystallization conditions, variable crystal, contacts, changes due to mutation, and varying attention to solvent during, crystallographic refinement, 62% of the 20 most frequently occupied sites, were conserved. Allowing for potential steric interference from, neighboring molecules in the crystal lattice, this fraction increased to, 79% of the sites. There was, however, no solvent-binding site that was, occupied in all 18 lysozyme molecules. A buried double site was occupied, in 17 instances and 2 other internal sites were occupied 15 times. Apart, from these buried sites, the most frequently occupied sites were often at, the amino-termini of alpha-helices. Solvent molecules at the most, conserved sites tended to have crystallographic thermal factors lower than, average, but atoms with low B-factors were not restricted to these sites., Although superficial inspection may suggest that only 50-60% (or less) of, solvent-binding sites are conserved in different crystal forms of a, protein, it appears that many sites appear to be empty either because of, steric interference or because the apparent occupancy of a given site can, vary from crystal to crystal. The X-ray method of identifying sites is, somewhat subjective and tends to result in specification only of those, solvent molecules that are well ordered and bound with high occupancy, even though there is clear evidence for solvent bound at many additional, sites.(ABSTRACT TRUNCATED AT 250 WORDS)

About this StructureAbout this Structure

152L is a Single protein structure of sequence from Enterobacteria phage t2 with SO4 as ligand. Active as Lysozyme, with EC number 3.2.1.17 Full crystallographic information is available from OCA.

ReferenceReference

Conservation of solvent-binding sites in 10 crystal forms of T4 lysozyme., Zhang XJ, Matthews BW, Protein Sci. 1994 Jul;3(7):1031-9. PMID:7920248

Page seeded by OCA on Tue Nov 20 10:27:52 2007

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

OCA