We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

2gnv

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2gnv.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2gnv.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2gnv| PDB=2gnv | SCENE= }}
{{STRUCTURE_2gnv| PDB=2gnv | SCENE= }}
-
'''Crystal structure of non-symbiotic plant hemoglobin from rice, B10 mutant F40L'''
+
===Crystal structure of non-symbiotic plant hemoglobin from rice, B10 mutant F40L===
-
==Overview==
+
<!--
-
All plants contain an unusual class of hemoglobins that display bis-histidyl coordination yet are able to bind exogenous ligands such as oxygen. Structurally homologous hexacoordinate hemoglobins (hxHbs) are also found in animals (neuroglobin and cytoglobin) and some cyanobacteria, where they are thought to play a role in free radical scavenging or ligand sensing. The plant hxHbs can be distinguished from the others because they are only weakly hexcacoordinate in the ferrous state, yet no structural mechanism for regulating hexacoordination has been articulated to account for this behavior. Plant hxHbs contain a conserved Phe at position B10 (Phe(B10)), which is near the reversibly coordinated distal His(E7). We have investigated the effects of Phe(B10) mutation on kinetic and equilibrium constants for hexacoordination and exogenous ligand binding in the ferrous and ferric oxidation states. Kinetic and equilibrium constants for hexacoordination and ligand binding along with CO-FTIR spectroscopy, midpoint reduction potentials, and the crystal structures of two key mutant proteins (F40W and F40L) reveal that Phe(B10) is an important regulatory element in hexacoordination. We show that Phe at this position is the only amino acid that facilitates stable oxygen binding to the ferrous Hb and the only one that promotes ligand binding in the ferric oxidation states. This work presents a structural mechanism for regulating reversible intramolecular coordination in plant hxHbs.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16893175}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16893175 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16893175}}
==About this Structure==
==About this Structure==
Line 31: Line 35:
[[Category: Nonsymbiotic]]
[[Category: Nonsymbiotic]]
[[Category: Rice]]
[[Category: Rice]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 05:19:21 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 17:03:22 2008''

Revision as of 14:03, 27 July 2008

Image:2gnv.png

Template:STRUCTURE 2gnv

Crystal structure of non-symbiotic plant hemoglobin from rice, B10 mutant F40L

Template:ABSTRACT PUBMED 16893175

About this Structure

2GNV is a Single protein structure of sequence from Oryza sativa. Full crystallographic information is available from OCA.

Reference

Role of phenylalanine B10 in plant nonsymbiotic hemoglobins., Smagghe BJ, Kundu S, Hoy JA, Halder P, Weiland TR, Savage A, Venugopal A, Goodman M, Premer S, Hargrove MS, Biochemistry. 2006 Aug 15;45(32):9735-45. PMID:16893175

Page seeded by OCA on Sun Jul 27 17:03:22 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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