1kr7

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[[Image:1kr7.jpg|left|200px]]<br /><applet load="1kr7" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1kr7.jpg|left|200px]]
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caption="1kr7, resolution 1.5&Aring;" />
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'''Crystal structure of the nerve tissue mini-hemoglobin from the nemertean worm Cerebratulus lacteus'''<br />
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{{Structure
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|PDB= 1kr7 |SIZE=350|CAPTION= <scene name='initialview01'>1kr7</scene>, resolution 1.5&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> and <scene name='pdbligand=OXY:OXYGEN MOLECULE'>OXY</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''Crystal structure of the nerve tissue mini-hemoglobin from the nemertean worm Cerebratulus lacteus'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1KR7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Cerebratulus_lacteus Cerebratulus lacteus] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=ACT:'>ACT</scene>, <scene name='pdbligand=HEM:'>HEM</scene> and <scene name='pdbligand=OXY:'>OXY</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KR7 OCA].
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1KR7 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Cerebratulus_lacteus Cerebratulus lacteus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KR7 OCA].
==Reference==
==Reference==
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The 109 residue nerve tissue minihemoglobin from Cerebratulus lacteus highlights striking structural plasticity of the alpha-helical globin fold., Pesce A, Nardini M, Dewilde S, Geuens E, Yamauchi K, Ascenzi P, Riggs AF, Moens L, Bolognesi M, Structure. 2002 May;10(5):725-35. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12015154 12015154]
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The 109 residue nerve tissue minihemoglobin from Cerebratulus lacteus highlights striking structural plasticity of the alpha-helical globin fold., Pesce A, Nardini M, Dewilde S, Geuens E, Yamauchi K, Ascenzi P, Riggs AF, Moens L, Bolognesi M, Structure. 2002 May;10(5):725-35. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12015154 12015154]
[[Category: Cerebratulus lacteus]]
[[Category: Cerebratulus lacteus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: nerve tissue]]
[[Category: nerve tissue]]
[[Category: oxygen transport]]
[[Category: oxygen transport]]
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[[Category: protein cavities]]
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[[Category: protein cavity]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:37:06 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:21:08 2008''

Revision as of 10:21, 20 March 2008


PDB ID 1kr7

Drag the structure with the mouse to rotate
, resolution 1.5Å
Ligands: , , and
Coordinates: save as pdb, mmCIF, xml



Crystal structure of the nerve tissue mini-hemoglobin from the nemertean worm Cerebratulus lacteus


Overview

A very short hemoglobin (CerHb; 109 amino acids) binds O(2) cooperatively in the nerve tissue of the nemertean worm Cerebratulus lacteus to sustain neural activity during anoxia. Sequence analysis suggests that CerHb tertiary structure may be unique among the known globin fold evolutionary variants. The X-ray structure of oxygenated CerHb (R factor 15.3%, at 1.5 A resolution) displays deletion of the globin N-terminal A helix, an extended GH region, a very short H helix, and heme solvent shielding based on specific aromatic residues. The heme-bound O(2) is stabilized by hydrogen bonds to the distal TyrB10-GlnE7 pair. Ligand access to heme may take place through a wide protein matrix tunnel connecting the distal site to a surface cleft located between the E and H helices.

About this Structure

1KR7 is a Single protein structure of sequence from Cerebratulus lacteus. Full crystallographic information is available from OCA.

Reference

The 109 residue nerve tissue minihemoglobin from Cerebratulus lacteus highlights striking structural plasticity of the alpha-helical globin fold., Pesce A, Nardini M, Dewilde S, Geuens E, Yamauchi K, Ascenzi P, Riggs AF, Moens L, Bolognesi M, Structure. 2002 May;10(5):725-35. PMID:12015154

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