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.


1k1y

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1k1y.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1k1y.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1k1y| PDB=1k1y | SCENE= }}
{{STRUCTURE_1k1y| PDB=1k1y | SCENE= }}
-
'''Crystal structure of thermococcus litoralis 4-alpha-glucanotransferase complexed with acarbose'''
+
===Crystal structure of thermococcus litoralis 4-alpha-glucanotransferase complexed with acarbose===
-
==Overview==
+
<!--
-
Thermococcus litoralis 4-alpha-glucanotransferase (TLGT) belongs to glucoside hydrolase family 57 and catalyzes the disproportionation of amylose and the formation of large cyclic alpha-1,4-glucan (cycloamylose) from linear amylose. We determined the crystal structure of TLGT with and without an inhibitor, acarbose. TLGT is composed of two domains: an N-terminal domain (domain I), which contains a (beta/alpha)7 barrel fold, and a C-terminal domain (domain II), which has a twisted beta-sandwich fold. In the structure of TLGT complexed with acarbose, the inhibitor was bound at the cleft within domain I, indicating that domain I is a catalytic domain of TLGT. The acarbose-bound structure also clarified that Glu123 and Asp214 were the catalytic nucleophile and acid/base catalyst, respectively, and revealed the residues involved in substrate binding. It seemed that TLGT produces large cyclic glucans by preventing the production of small cyclic glucans by steric hindrance, which is achieved by three lids protruding into the active site cleft, as well as an extended active site cleft. Interestingly, domain I of TLGT shares some structural features with the catalytic domain of Golgi alpha-mannosidase from Drosophila melanogaster, which belongs to glucoside hydrolase family 38. Furthermore, the catalytic residue of the two enzymes is located in the same position. These observations suggest that families 57 and 38 evolved from a common ancestor.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12618437}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12618437 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12618437}}
==About this Structure==
==About this Structure==
Line 31: Line 35:
[[Category: Yamamoto, M.]]
[[Category: Yamamoto, M.]]
[[Category: 4-alpha-glucanotransferase complexed with acarbose]]
[[Category: 4-alpha-glucanotransferase complexed with acarbose]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:11:58 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 21:20:34 2008''

Revision as of 18:20, 1 July 2008

Image:1k1y.png

Template:STRUCTURE 1k1y

Crystal structure of thermococcus litoralis 4-alpha-glucanotransferase complexed with acarbose

Template:ABSTRACT PUBMED 12618437

About this Structure

1K1Y is a Single protein structure of sequence from Thermococcus litoralis. Full crystallographic information is available from OCA.

Reference

Crystal structures of 4-alpha-glucanotransferase from Thermococcus litoralis and its complex with an inhibitor., Imamura H, Fushinobu S, Yamamoto M, Kumasaka T, Jeon BS, Wakagi T, Matsuzawa H, J Biol Chem. 2003 May 23;278(21):19378-86. Epub 2003 Mar 4. PMID:12618437

Page seeded by OCA on Tue Jul 1 21:20:34 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1k1y"
Personal tools