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.


1x9u

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1x9u.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1x9u.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1x9u| PDB=1x9u | SCENE= }}
{{STRUCTURE_1x9u| PDB=1x9u | SCENE= }}
-
'''Umecyanin from Horse Raddish- Crystal Structure of the reduced form'''
+
===Umecyanin from Horse Raddish- Crystal Structure of the reduced form===
-
==Overview==
+
<!--
-
Umecyanin (UMC) is a type 1 copper-containing protein which originates from horseradish roots and belongs to the stellacyanin subclass of the phytocyanins, a ubiquitous family of plant cupredoxins. The crystal structures of Cu(II) and Cu(I) UMC have been determined at 1.9 and 1.8 A, respectively. The protein has an overall fold similar to those of other phytocyanins. At the active site the cupric ion is coordinated by the N(delta1) atoms of His44 and His90, the S(gamma) of Cys85, and the O(epsilon)(1) of Gln95 in a distorted tetrahedral geometry. Both His ligands are solvent exposed and are surrounded by nonpolar and polar side chains on the protein surface. Thus, UMC does not possess a distinct hydrophobic patch close to the active site in contrast to almost all other cupredoxins. UMC has a large surface acidic patch situated approximately 10-30 A from the active site. The structure of Cu(I) UMC is the first determined for a reduced phytocyanin and demonstrates that the coordination environment of the cuprous ion is more trigonal pyramidal. This subtle change in geometry is primarily due to the Cu-N(delta1)(His44) and Cu-O(epsilon1)(Gln95) bond lengths increasing from 2.0 and 2.3 A in Cu(II) UMC to 2.2 and 2.5 A, respectively, in the reduced form, as a consequence of slight rotations of the His44 and Gln95 side chains. The limited structural changes upon redox interconversion at the active site of this stellacyanin are analogous to those observed in a typical type 1 copper site with an axial Met ligand and along with its surface features suggest a role for UMC in interprotein electron transfer.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15631465}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15631465 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15631465}}
==About this Structure==
==About this Structure==
Line 34: Line 38:
[[Category: Phytocyanin]]
[[Category: Phytocyanin]]
[[Category: Umecyanin]]
[[Category: Umecyanin]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 14:45:28 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 12:22:21 2008''

Revision as of 09:22, 29 July 2008

Image:1x9u.png

Template:STRUCTURE 1x9u

Umecyanin from Horse Raddish- Crystal Structure of the reduced form

Template:ABSTRACT PUBMED 15631465

About this Structure

1X9U is a Single protein structure of sequence from Armoracia rusticana. Full crystallographic information is available from OCA.

Reference

Crystal structures of oxidized and reduced stellacyanin from horseradish roots., Koch M, Velarde M, Harrison MD, Echt S, Fischer M, Messerschmidt A, Dennison C, J Am Chem Soc. 2005 Jan 12;127(1):158-66. PMID:15631465

Page seeded by OCA on Tue Jul 29 12:22:21 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1x9u"
Personal tools