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.


2c81

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2c81.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2c81.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2c81| PDB=2c81 | SCENE= }}
{{STRUCTURE_2c81| PDB=2c81 | SCENE= }}
-
'''CRYSTAL STRUCTURES OF THE PLP- AND PMP-BOUND FORMS OF BTRR, A DUAL FUNCTIONAL AMINOTRANSFERASE INVOLVED IN BUTIROSIN BIOSYNTHESIS.'''
+
===CRYSTAL STRUCTURES OF THE PLP- AND PMP-BOUND FORMS OF BTRR, A DUAL FUNCTIONAL AMINOTRANSFERASE INVOLVED IN BUTIROSIN BIOSYNTHESIS.===
-
==Overview==
+
<!--
-
The aminotransferase (BtrR), which is involved in the biosynthesis of butirosin, a 2-deoxystreptamine (2-DOS)-containing aminoglycoside antibiotic produced by Bacillus circulans, catalyses the pyridoxal phosphate (PLP)-dependent transamination reaction both of 2-deoxy-scyllo-inosose to 2-deoxy-scyllo-inosamine and of amino-dideoxy-scyllo-inosose to 2-DOS. The high-resolution crystal structures of the PLP- and PMP-bound forms of BtrR aminotransferase from B. circulans were solved at resolutions of 2.1 A and 1.7 A with R(factor)/R(free) values of 17.4/20.6 and 19.9/21.9, respectively. BtrR has a fold characteristic of the aspartate aminotransferase family, and sequence and structure analysis categorises it as a member of SMAT (secondary metabolite aminotransferases) subfamily. It exists as a homodimer with two active sites per dimer. The active site of the BtrR protomer is located in a cleft between an alpha helical N-terminus, a central alphabetaalpha sandwich domain and an alphabeta C-terminal domain. The structures of the PLP- and PMP-bound enzymes are very similar; however BtrR-PMP lacks the covalent bond to Lys192. Furthermore, the two forms differ in the side-chain conformations of Trp92, Asp163, and Tyr342 that are likely to be important in substrate selectivity and substrate binding. This is the first three-dimensional structure of an enzyme from the butirosin biosynthesis gene cluster.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16894611}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16894611 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16894611}}
==About this Structure==
==About this Structure==
Line 33: Line 37:
[[Category: Smat]]
[[Category: Smat]]
[[Category: Transferase]]
[[Category: Transferase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 21:25:18 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 10:02:28 2008''

Revision as of 07:02, 29 July 2008

Image:2c81.png

Template:STRUCTURE 2c81

CRYSTAL STRUCTURES OF THE PLP- AND PMP-BOUND FORMS OF BTRR, A DUAL FUNCTIONAL AMINOTRANSFERASE INVOLVED IN BUTIROSIN BIOSYNTHESIS.

Template:ABSTRACT PUBMED 16894611

About this Structure

2C81 is a Single protein structure of sequence from Bacillus circulans. Full crystallographic information is available from OCA.

Reference

Crystal structures of the PLP- and PMP-bound forms of BtrR, a dual functional aminotransferase involved in butirosin biosynthesis., Popovic B, Tang X, Chirgadze DY, Huang F, Blundell TL, Spencer JB, Proteins. 2006 Oct 1;65(1):220-30. PMID:16894611

Page seeded by OCA on Tue Jul 29 10:02:28 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2c81"
Personal tools