2bk9

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==About this Structure==
==About this Structure==
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2BK9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=HEM:'>HEM</scene> and <scene name='pdbligand=CXS:'>CXS</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Sites: <scene name='pdbsite=AC1:Hem Binding Site For Chain A'>AC1</scene>, <scene name='pdbsite=AC2:Cxs Binding Site For Chain A'>AC2</scene> and <scene name='pdbsite=AC3:Cl Binding Site For Chain A'>AC3</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BK9 OCA].
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2BK9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=HEM:'>HEM</scene> and <scene name='pdbligand=CXS:'>CXS</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Sites: <scene name='pdbsite=AC1:Hem+Binding+Site+For+Chain+A'>AC1</scene>, <scene name='pdbsite=AC2:Cxs+Binding+Site+For+Chain+A'>AC2</scene> and <scene name='pdbsite=AC3:Cl+Binding+Site+For+Chain+A'>AC3</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BK9 OCA].
==Reference==
==Reference==
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[[Category: protein structure oxygen transport]]
[[Category: protein structure oxygen transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 12:19:05 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:25:03 2008''

Revision as of 08:25, 3 February 2008


2bk9, resolution 1.20Å

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DROSOPHILA MELANOGASTER GLOBIN

Overview

Hemoglobins at high concentration have been isolated long ago from some, insect larvae living in hypoxic environments. Conversely, a monomeric, hemoglobin has been discovered recently in the fruit fly Drosophila, melanogaster as intracellular protein expressed both in larvae and in the, adult fly. Such a finding indicates that the oxygen supply in insects may, be more complex than previously thought, relying not only on O2 diffusion, through the tubular tracheal system, but also on carrier-mediated, transport and storage. We present here the crystal structure of, recombinant D. melanogaster hemoglobin at 1.20 A resolution. Spectroscopic, data show that the protein displays a hexacoordinated heme, whose axial, ligands are the proximal and distal His residues. Such bis-His ligation of, the heme has sizable effects on the protein local structure. Three protein, matrix cavities, comparable in size but not in topological locations with, those of sperm whale myoglobin, are spread through the protein matrix; one, of these can host a xenon atom. Additionally, D. melanogaster hemoglobin, binds one molecule of 3-(cyclohexylamino)propanesulfonic acid (CAPS), buffer at a surface pocket, next to the EF hinge. Despite the high, resolution achieved, no sequence/structure features specifically, supporting the heme hexa- to pentacoordination transition required for, diatomic ligand binding could be recognized.

About this Structure

2BK9 is a Single protein structure of sequence from Drosophila melanogaster with , , and as ligands. Known structural/functional Sites: , and . Full crystallographic information is available from OCA.

Reference

Bishistidyl heme hexacoordination, a key structural property in Drosophila melanogaster hemoglobin., de Sanctis D, Dewilde S, Vonrhein C, Pesce A, Moens L, Ascenzi P, Hankeln T, Burmester T, Ponassi M, Nardini M, Bolognesi M, J Biol Chem. 2005 Jul 22;280(29):27222-9. Epub 2005 May 24. PMID:15917230

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