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.


1qhb

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1qhb.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1qhb.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1qhb| PDB=1qhb | SCENE= }}
{{STRUCTURE_1qhb| PDB=1qhb | SCENE= }}
-
'''VANADIUM BROMOPEROXIDASE FROM RED ALGA CORALLINA OFFICINALIS'''
+
===VANADIUM BROMOPEROXIDASE FROM RED ALGA CORALLINA OFFICINALIS===
-
==Overview==
+
<!--
-
The three-dimensional structure of the vanadium bromoperoxidase protein from the marine red macroalgae Corallina officinalis has been determined by single isomorphous replacement at 2.3 A resolution. The enzyme subunit is made up of 595 amino acid residues folded into a single alpha+beta domain. There are 12 bromoperoxidase subunits, arranged with 23-point group symmetry. A cavity is formed by the N terminus of each subunit in the centre of the dodecamer. The subunit fold and dimer organisation of the Cor. officinalis vanadium bromoperoxidase are similar to those of the dimeric enzyme from the brown algae Ascophyllum nodosum, with which it shares 33 % sequence identity. The different oligomeric state of the two algal enzymes seems to reflect separate mechanisms of adaptation to harsh environmental conditions and/or to chemically active substrates and products. The residues involved in the vanadate binding are conserved between the two algal bromoperoxidases and the vanadium chloroperoxidase from the fungus Curvularia inaequalis. However, most of the other residues forming the active-site cavity are different in the three enzymes, which reflects differences in the substrate specificity and stereoselectivity of the reaction. A dimer of the Cor. officinalis enzyme partially superimposes with the two-domain monomer of the fungal enzyme.
+
The line below this paragraph, {{ABSTRACT_PUBMED_10843856}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 10843856 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_10843856}}
==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Red alga]]
[[Category: Red alga]]
[[Category: Vanadium-dependent]]
[[Category: Vanadium-dependent]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:16:21 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 06:03:16 2008''

Revision as of 03:03, 29 July 2008

Image:1qhb.png

Template:STRUCTURE 1qhb

VANADIUM BROMOPEROXIDASE FROM RED ALGA CORALLINA OFFICINALIS

Template:ABSTRACT PUBMED 10843856

About this Structure

1QHB is a Single protein structure of sequence from Corallina officinalis. Full crystallographic information is available from OCA.

Reference

Crystal structure of dodecameric vanadium-dependent bromoperoxidase from the red algae Corallina officinalis., Isupov MN, Dalby AR, Brindley AA, Izumi Y, Tanabe T, Murshudov GN, Littlechild JA, J Mol Biol. 2000 Jun 16;299(4):1035-49. PMID:10843856

Page seeded by OCA on Tue Jul 29 06:03:16 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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