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.


1hze

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1hze.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1hze.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1hze| PDB=1hze | SCENE= }}
{{STRUCTURE_1hze| PDB=1hze | SCENE= }}
-
'''SOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN OF RIBOFLAVIN SYNTHASE FROM E. COLI'''
+
===SOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN OF RIBOFLAVIN SYNTHASE FROM E. COLI===
-
==Overview==
+
<!--
-
The structure of the amino-terminal domain of Escherichia coli riboflavin synthase (RiSy) has been determined by NMR spectroscopy with riboflavin as a bound ligand. RiSy is functional as a 75 kDa homotrimer, each subunit of which consists of two domains which share very similar sequences and structures. The N-terminal domain (RiSy-N; 97 residues) forms a 20 kDa homodimer in solution which binds riboflavin with high affinity. The structure features a six-stranded antiparallel beta-barrel with a Greek-key fold, both ends of which are closed by an alpha-helix. One riboflavin molecule is bound per monomer in a site at one end of the barrel which is comprised of elements of both monomers. The structure and ligand binding are similar to that of the FAD binding domains of ferrodoxin reductase family proteins. The structure provides insights into the structure of the whole enzyme, the organisation of the functional trimer and the mechanism of riboflavin synthesis. C48 from the N-terminal domain is identified as the free cysteine implicated in a nucleophilic role in the synthesis mechanism, while H102 from the C-terminal domains is also likely to play a key role. Both are invariant in all known riboflavin synthase sequences.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11399071}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11399071 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11399071}}
==About this Structure==
==About this Structure==
-
1HZE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HZE OCA].
+
1HZE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HZE OCA].
==Reference==
==Reference==
Line 32: Line 36:
[[Category: Truffault, V.]]
[[Category: Truffault, V.]]
[[Category: Greek-key-barrel]]
[[Category: Greek-key-barrel]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:23:39 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 10:10:36 2008''

Revision as of 07:10, 1 July 2008

Image:1hze.png

Template:STRUCTURE 1hze

SOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN OF RIBOFLAVIN SYNTHASE FROM E. COLI

Template:ABSTRACT PUBMED 11399071

About this Structure

1HZE is a Single protein structure of sequence from Escherichia coli. Full experimental information is available from OCA.

Reference

The solution structure of the N-terminal domain of riboflavin synthase., Truffault V, Coles M, Diercks T, Abelmann K, Eberhardt S, Luttgen H, Bacher A, Kessler H, J Mol Biol. 2001 Jun 15;309(4):949-60. PMID:11399071

Page seeded by OCA on Tue Jul 1 10:10:36 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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