1kr7

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{{Seed}}
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{{STRUCTURE_1kr7| PDB=1kr7 | SCENE= }}
{{STRUCTURE_1kr7| PDB=1kr7 | SCENE= }}
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'''Crystal structure of the nerve tissue mini-hemoglobin from the nemertean worm Cerebratulus lacteus'''
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===Crystal structure of the nerve tissue mini-hemoglobin from the nemertean worm Cerebratulus lacteus===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 12015154 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12015154}}
==About this Structure==
==About this Structure==
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[[Category: Oxygen transport]]
[[Category: Oxygen transport]]
[[Category: Protein cavity]]
[[Category: Protein cavity]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:04:32 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 10:49:31 2008''

Revision as of 07:49, 2 July 2008

Image:1kr7.png

Template:STRUCTURE 1kr7

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

Template:ABSTRACT PUBMED 12015154

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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