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.


1yna

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1yna.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1yna.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1yna| PDB=1yna | SCENE= }}
{{STRUCTURE_1yna| PDB=1yna | SCENE= }}
-
'''ENDO-1,4-BETA-XYLANASE, ROOM TEMPERATURE, PH 4.0'''
+
===ENDO-1,4-BETA-XYLANASE, ROOM TEMPERATURE, PH 4.0===
-
==Overview==
+
<!--
-
The crystal structure of the thermostable xylanase from Thermomyces lanuginosus was determined by single-crystal X-ray diffraction. The protein crystallizes in space group P21, a = 40.96(4) A, b = 52. 57(5) A, c = 50.47 (5) A, beta = 100.43(5) degrees, Z = 2. Diffraction data were collected at room temperature for a resolution range of 25-1.55 A, and the structure was solved by molecular replacement with the coordinates of xylanase II from Trichoderma reesei as a search model and refined to a crystallographic R-factor of 0.155 for all observed reflections. The enzyme belongs to the family 11 of glycosyl hydrolases [Henrissat, B., and Bairoch, A. (1993) Biochem. J. 293, 781-788]. pKa calculations were performed to assess the protonation state of residues relevant for catalysis and enzyme stability, and a heptaxylan was fitted into the active-site groove by homology modeling, using the published crystal structure of a complex between the Bacillus circulans xylanase and a xylotetraose. Molecular dynamics indicated the central three sugar rings to be tightly bound, whereas the peripheral ones can assume different orientations and conformations, suggesting that the enzyme might also accept xylan chains which are branched at these positions. The reasons for the thermostability of the T. lanuginosus xylanase were analyzed by comparing its crystal structure with known structures of mesophilic family 11 xylanases. It appears that the thermostability is due to the presence of an extra disulfide bridge, as well as to an increase in the density of charged residues throughout the protein.
+
The line below this paragraph, {{ABSTRACT_PUBMED_9753433}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 9753433 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_9753433}}
==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: Xylanase]]
[[Category: Xylanase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:32:17 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 23:46:17 2008''

Revision as of 20:46, 28 July 2008

Image:1yna.png

Template:STRUCTURE 1yna

ENDO-1,4-BETA-XYLANASE, ROOM TEMPERATURE, PH 4.0

Template:ABSTRACT PUBMED 9753433

About this Structure

1YNA is a Single protein structure of sequence from Thermomyces lanuginosus. Full crystallographic information is available from OCA.

Reference

Thermophilic xylanase from Thermomyces lanuginosus: high-resolution X-ray structure and modeling studies., Gruber K, Klintschar G, Hayn M, Schlacher A, Steiner W, Kratky C, Biochemistry. 1998 Sep 29;37(39):13475-85. PMID:9753433

Page seeded by OCA on Mon Jul 28 23:46:17 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1yna"
Personal tools