1clk: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
Line 1: Line 1:
[[Image:1clk.gif|left|200px]]
{{Seed}}
[[Image:1clk.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1clk|  PDB=1clk  |  SCENE=  }}  
{{STRUCTURE_1clk|  PDB=1clk  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF STREPTOMYCES DIASTATICUS NO.7 STRAIN M1033 XYLOSE ISOMERASE AT 1.9 A RESOLUTION WITH PSEUDO-I222 SPACE GROUP'''
===CRYSTAL STRUCTURE OF STREPTOMYCES DIASTATICUS NO.7 STRAIN M1033 XYLOSE ISOMERASE AT 1.9 A RESOLUTION WITH PSEUDO-I222 SPACE GROUP===




==Overview==
<!--
The structure of xylose isomerase (XyI) from Streptomyces diastaticus No. 7 strain M1033 (SDXyI) has been refined at 1.85 A resolution to conventional and free R factors of 0.166 and 0.219, respectively. SDXyI was crystallized in space group P2(1)2(1)2, with unit-cell parameters a = 87.976, b = 98.836, c = 93.927 A. One dimer of the tetrametric molecule is found in each asymmetric unit. Each monomer consists of two domains: a large N-terminal domain (residues 1-320), containing a parallel eight-stranded alpha/beta barrel, and a small C-terminal loop (residues 321-387), containing five helices linked by random coil. The four monomers are essentially identical in the tetramer, possessing non-crystallographic 222 symmetry with one twofold axis essentially coincident with the crystallographic twofold axis in the space group P2(1)2(1)2, which may explain why the diffraction pattern has strong pseudo-I222 symmetry even at medium resolution. The crystal structures of XyIs from different bacterial strains, especially from Streptomyces, are similar. The alpha2 helix of the alpha/beta barrel has a different position in the structures of different XyIs. The conformation of C-terminal fragment 357-364 in the SDXyI structure has a small number of differences to that of other XyIs. Two Co(2+) ions rather than Mg(2+) ions exist in the active site of the SDXyI structure; SDXyI seems to prefer to bind Co(2+) ions rather than Mg(2+) ions.
The line below this paragraph, {{ABSTRACT_PUBMED_10666592}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 10666592 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_10666592}}


==About this Structure==
==About this Structure==
Line 33: Line 37:
[[Category: Streptomyce]]
[[Category: Streptomyce]]
[[Category: Xylose isomerase]]
[[Category: Xylose isomerase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 12:51:52 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:54:58 2008''

Revision as of 17:54, 30 June 2008

File:1clk.png

Template:STRUCTURE 1clk

CRYSTAL STRUCTURE OF STREPTOMYCES DIASTATICUS NO.7 STRAIN M1033 XYLOSE ISOMERASE AT 1.9 A RESOLUTION WITH PSEUDO-I222 SPACE GROUP

Template:ABSTRACT PUBMED 10666592

About this Structure

1CLK is a Single protein structure of sequence from Streptomyces diastaticus. Full crystallographic information is available from OCA.

Reference

Structure of xylose isomerase from Streptomyces diastaticus no. 7 strain M1033 at 1.85 A resolution., Zhu X, Teng M, Niu L, Xu C, Wang Y, Acta Crystallogr D Biol Crystallogr. 2000 Feb;56(Pt 2):129-36. PMID:10666592

Page seeded by OCA on Mon Jun 30 20:54:58 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1clk&oldid=583195"