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.


1ns6

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1ns6.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1ns6.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1ns6| PDB=1ns6 | SCENE= }}
{{STRUCTURE_1ns6| PDB=1ns6 | SCENE= }}
-
'''The 2.1A Structure of Horse (alpha hemichrome/beta met) Hemoglobin at pH 5.4'''
+
===The 2.1A Structure of Horse (alpha hemichrome/beta met) Hemoglobin at pH 5.4===
-
==Overview==
+
<!--
-
In 1947, Perutz and co-workers reported that crystalline horse methemoglobin undergoes a large lattice transition as the pH is decreased from 7.1 to 5.4. We have determined the pH 7.1 and 5.4 crystal structures of horse methemoglobin at 1.6 and 2.1 A resolution, respectively, and find that this lattice transition involves a 23 A translation of adjacent hemoglobin tetramers as well as changes in alpha heme ligation and the tertiary structure of the alpha subunits. Specifically, when the pH is lowered from 7.1 to 5.4, the Fe(3+) alpha heme groups (but not the beta heme groups) are converted from the aquomet form, in which the proximal histidine [His87(F8)alpha] and a water molecule are the axial heme ligands, to the hemichrome (bishistidine) form, in which the proximal histidine and the distal histidine [His58(E7)alpha] are the axial heme ligands. Hemichrome formation is coupled to a large tertiary structure transition in the eight-residue segment Pro44(CD2)alpha-Gly51(D7)alpha that converts from an extended loop structure at pH 7.1 to a pi-like helix at pH 5.4. The formation of the pi helix forces Phe46(CD4)alpha out of the alpha heme pocket and into the interface between adjacent hemoglobin tetramers where it participates in crystal lattice contacts unique to the pH 5.4 structure. In addition, the transition from aquomet alpha subunits to bishistidine alpha subunits is accompanied by an approximately 1.2 A movement of the alpha heme groups to a more solvent-exposed position as well as the creation of a solvent channel from the interior of the alpha heme pocket to the outside of the tetramer. These changes and the extensive rearrangement of the crystal lattice structure allow the alpha heme group of one tetramer to make direct contact with an alpha heme group on an adjacent tetramer. These results suggest possible functional roles for hemichrome formation in vivo.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12939139}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12939139 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12939139}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Globin fold]]
[[Category: Globin fold]]
[[Category: Hemichrome]]
[[Category: Hemichrome]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:54:56 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 05:26:28 2008''

Revision as of 02:26, 29 July 2008

Image:1ns6.png

Template:STRUCTURE 1ns6

The 2.1A Structure of Horse (alpha hemichrome/beta met) Hemoglobin at pH 5.4

Template:ABSTRACT PUBMED 12939139

About this Structure

1NS6 is a Protein complex structure of sequences from Equus caballus. Full crystallographic information is available from OCA.

Reference

A pH-dependent aquomet-to-hemichrome transition in crystalline horse methemoglobin., Robinson VL, Smith BB, Arnone A, Biochemistry. 2003 Sep 2;42(34):10113-25. PMID:12939139

Page seeded by OCA on Tue Jul 29 05:26:28 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ns6"
Personal tools