This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1clk

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
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

Image: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 "http://52.214.119.220/wiki/index.php/1clk"
Personal tools