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.


3c2u

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px <!-- The line below this paragraph, containing "STRUCTURE_3c2u", creates the "Structure Box" on the page. You may change the PDB parameter (which sets the PD...)
Line 1: Line 1:
-
[[Image:3c2u.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:3c2u.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_3c2u| PDB=3c2u | SCENE= }}
{{STRUCTURE_3c2u| PDB=3c2u | SCENE= }}
-
'''Structure of the two subsite D-xylosidase from Selenomonas ruminantium in complex with 1,3-bis[tris(hydroxymethyl)methylamino]propane'''
+
===Structure of the two subsite D-xylosidase from Selenomonas ruminantium in complex with 1,3-bis[tris(hydroxymethyl)methylamino]propane===
-
==Overview==
+
<!--
-
The three-dimensional structure of the catalytically efficient beta-xylosidase from Selenomonas ruminantium in complex with competitive inhibitor 1,3-bis[tris(hydroxymethyl)methylamino]propane (BTP) was determined by using X-ray crystallography (1.3A resolution). Most H bonds between inhibitor and protein occur within subsite -1, including one between the carboxyl group of E186 and an N group of BTP. The other N of BTP occupies subsite +1 near K99. E186 (pK(a) 7.2) serves as catalytic acid. The pH (6-10) profile for 1/K(i)((BTP)) is bell-shaped with pK(a)'s 6.8 and 7.8 on the acidic limb assigned to E186 and inhibitor groups and 9.9 on the basic limb assigned to inhibitor. Mutation K99A eliminates pK(a) 7.8, strongly suggesting that the BTP monocation binds to the dianionic enzyme D14(-)E186(-). A sedimentation equilibrium experiment estimates a K(d) ([dimer](2)/[tetramer]) of 7x10(-9)M. Similar k(cat) and k(cat)/K(m) values were determined when the tetramer/dimer ratio changes from 0.0028 to 26 suggesting that dimers and tetramers are equally active forms.
+
The line below this paragraph, {{ABSTRACT_PUBMED_18374656}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 18374656 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_18374656}}
==About this Structure==
==About this Structure==
Line 31: Line 35:
[[Category: Glycoside hydrolase]]
[[Category: Glycoside hydrolase]]
[[Category: Tetramer]]
[[Category: Tetramer]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr 24 09:51:30 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 10:23:36 2008''

Revision as of 07:23, 28 July 2008

Image:3c2u.png

Template:STRUCTURE 3c2u

Structure of the two subsite D-xylosidase from Selenomonas ruminantium in complex with 1,3-bis[tris(hydroxymethyl)methylamino]propane

Template:ABSTRACT PUBMED 18374656

About this Structure

3C2U is a Single protein structure of sequence from Selenomonas ruminantium. Full crystallographic information is available from OCA.

Reference

Structure of the two-subsite beta-d-xylosidase from Selenomonas ruminantium in complex with 1,3-bis[tris(hydroxymethyl)methylamino]propane., Brunzelle JS, Jordan DB, McCaslin DR, Olczak A, Wawrzak Z, Arch Biochem Biophys. 2008 Mar 14;. PMID:18374656

Page seeded by OCA on Mon Jul 28 10:23:36 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3c2u"
Personal tools