2h8f: Difference between revisions

Revision as of 00:21, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2h8f.png

Template:STRUCTURE 2h8f

Crystal structure of deoxy hemoglobin from Trematomus bernacchii at pH 6.2Crystal structure of deoxy hemoglobin from Trematomus bernacchii at pH 6.2

Template:ABSTRACT PUBMED 16909420

About this StructureAbout this Structure

2H8F is a Protein complex structure of sequences from Trematomus bernacchii. Full crystallographic information is available from OCA.

ReferenceReference

High resolution crystal structure of deoxy hemoglobin from Trematomus bernacchii at different pH values: the role of histidine residues in modulating the strength of the root effect., Mazzarella L, Vergara A, Vitagliano L, Merlino A, Bonomi G, Scala S, Verde C, di Prisco G, Proteins. 2006 Nov 1;65(2):490-8. PMID:16909420

Minimal structural requirements for root effect: crystal structure of the cathodic hemoglobin isolated from the antarctic fish Trematomus newnesi., Mazzarella L, Bonomi G, Lubrano MC, Merlino A, Riccio A, Vergara A, Vitagliano L, Verde C, di Prisco G, Proteins. 2006 Feb 1;62(2):316-21. PMID:16299734

Crystal structure of Trematomus newnesi haemoglobin re-opens the root effect question., Mazzarella L, D'Avino R, di Prisco G, Savino C, Vitagliano L, Moody PC, Zagari A, J Mol Biol. 1999 Apr 16;287(5):897-906. PMID:10222199

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 {{STRUCTURE_2h8f|  PDB=2h8f  |  SCENE=  }}
-'''Crystal structure of deoxy hemoglobin from Trematomus bernacchii at pH 6.2'''
+===Crystal structure of deoxy hemoglobin from Trematomus bernacchii at pH 6.2===
-==Overview==
+<!--
-The Root effect is a widespread property in fish hemoglobins (Hbs) that produces a drastic reduction of cooperativity and oxygen-binding ability at acidic pH. Here, we report the high-resolution structure of the deoxy form of Hb isolated from the Antarctic fish Trematomus bernacchii (HbTb) crystallized at pH 6.2 and 8.4. The structure at acidic pH has been previously determined at a moderate resolution (Ito et al., J Mol Biol 1995;250:648-658). Our results provide a clear picture of the events occurring upon the pH increase from 6.2 to 8.4, observed within a practically unchanged crystal environment. In particular, at pH 8.4, the interaspartic hydrogen bond at the alpha(1)beta(2) interface is partially broken, suggesting a pK(a) close to 8.4 for Asp95alpha. In addition, a detailed survey of the histidine modifications, caused by the change in pH, also indicates that at least three hot regions of the molecule are modified (Ebeta helix, Cbeta-tail, CDalpha corner) and can be considered to be involved at various levels in the release of the Root protons. Most importantly, at the CDalpha corner, the break of the salt bridge Asp48alpha-His55alpha allows us to describe a detailed mechanism that transmits the modification from the CDalpha corner far to the alpha heme. More generally, the results shed light on the role played by the histidine residues in modulating the strength of the Root effect and also support the emerging idea that the structural determinants, at least for a part of the Root effect, are specific of each Hb endowed with this property.
+The line below this paragraph, {{ABSTRACT_PUBMED_16909420}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16909420 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16909420}}
 ==About this Structure==
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 ==Reference==
 High resolution crystal structure of deoxy hemoglobin from Trematomus bernacchii at different pH values: the role of histidine residues in modulating the strength of the root effect., Mazzarella L, Vergara A, Vitagliano L, Merlino A, Bonomi G, Scala S, Verde C, di Prisco G, Proteins. 2006 Nov 1;65(2):490-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16909420 16909420]
+Minimal structural requirements for root effect: crystal structure of the cathodic hemoglobin isolated from the antarctic fish Trematomus newnesi., Mazzarella L, Bonomi G, Lubrano MC, Merlino A, Riccio A, Vergara A, Vitagliano L, Verde C, di Prisco G, Proteins. 2006 Feb 1;62(2):316-21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16299734 16299734]
+Crystal structure of Trematomus newnesi haemoglobin re-opens the root effect question., Mazzarella L, D'Avino R, di Prisco G, Savino C, Vitagliano L, Moody PC, Zagari A, J Mol Biol. 1999 Apr 16;287(5):897-906. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10222199 10222199]
 [[Category: Protein complex]]
 [[Category: Trematomus bernacchii]]
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 [[Category: Ph]]
 [[Category: Root effect]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 05:59:24 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 00:21:56 2008''