3c2u: Difference between revisions

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{{STRUCTURE_3c2u|  PDB=3c2u  |  SCENE=  }}  
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'''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==
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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.
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==About this Structure==
==About this Structure==
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[[Category: Glycoside hydrolase]]
[[Category: Glycoside hydrolase]]
[[Category: Tetramer]]
[[Category: Tetramer]]
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Revision as of 07:23, 28 July 2008

File: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

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