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.




1ith

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1ith.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1ith.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1ith| PDB=1ith | SCENE= }}
{{STRUCTURE_1ith| PDB=1ith | SCENE= }}
-
'''STRUCTURE DETERMINATION AND REFINEMENT OF HOMOTETRAMERIC HEMOGLOBIN FROM URECHIS CAUPO AT 2.5 ANGSTROMS RESOLUTION'''
+
===STRUCTURE DETERMINATION AND REFINEMENT OF HOMOTETRAMERIC HEMOGLOBIN FROM URECHIS CAUPO AT 2.5 ANGSTROMS RESOLUTION===
-
==Overview==
+
<!--
-
A 5 A resolution multiple isomorphous replacement solution for hemoglobin isolated from Urechis caupo revealed a previously unobserved quaternary structure for tetrameric hemoglobin [Kolatkar, Meador, Stanfield &amp; Hackert (1988). J. Biol. Chem. 263(7), 3462-3465]. We report here the structure of Urechis hemoglobin in the cyanomet state refined to 2.5 A resolution by simulated annealing yielding R = 0.148 for reflections F greater than 3 sigma between 5.0 and 2.5 A resolution. The starting model was fitted to a map originally derived from multiple-wavelength anomalous-dispersion phases to 3 A resolution that was then subjected to cyclic twofold molecular averaging and solvent flattening. Structural analysis of the resultant model shows that the unique quaternary assemblage is possible due to several favorable interactions between subunits, including salt links, hydrophobic pockets and interactions mediated by bound water. The tetramer is stabilized by subunit-subunit interactions between the G/H turns and D helices within the crystallographic dimer, and the A/B turn regions and E helices between subunits related by a molecular twofold axis. Interestingly, each subunit has one cysteine residue (Cys21) located in the A/B turn. These twofold-related cysteinyl residues are near enough to one another to form a disulfide bridge but do not.
+
The line below this paragraph, {{ABSTRACT_PUBMED_1515107}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 1515107 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_1515107}}
==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Phizackerley, R P.]]
[[Category: Phizackerley, R P.]]
[[Category: Oxygen transport]]
[[Category: Oxygen transport]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:23:39 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 13:58:24 2008''

Revision as of 10:58, 1 July 2008

Image:1ith.png

Template:STRUCTURE 1ith

STRUCTURE DETERMINATION AND REFINEMENT OF HOMOTETRAMERIC HEMOGLOBIN FROM URECHIS CAUPO AT 2.5 ANGSTROMS RESOLUTION

Template:ABSTRACT PUBMED 1515107

About this Structure

1ITH is a Single protein structure of sequence from Urechis caupo. Full crystallographic information is available from OCA.

Reference

Structure determination and refinement of homotetrameric hemoglobin from Urechis caupo at 2.5 A resolution., Kolatkar PR, Ernst SR, Hackert ML, Ogata CM, Hendrickson WA, Merritt EA, Phizackerley RP, Acta Crystallogr B. 1992 Apr 1;48 ( Pt 2):191-9. PMID:1515107

Page seeded by OCA on Tue Jul 1 13:58:24 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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