1kfr: Difference between revisions

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[[Image:1kfr.jpg|left|200px]]
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{{STRUCTURE_1kfr|  PDB=1kfr  |  SCENE=  }}  
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'''Structural plasticity in the eight-helix fold of a trematode hemoglobin'''
===Structural plasticity in the eight-helix fold of a trematode hemoglobin===




==Overview==
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The three-dimensional structure of recombinant haemoglobin from the trematode Paramphistomum epiclitum, displaying the highest oxygen affinity so far observed for (non)vertebrate haemoglobins, has previously been determined at 1.17 A resolution (orthorhombic space group P2(1)2(1)2(1)). In the present communication, the three-dimensional structure of wild-type P. epiclitum haemoglobin is reported at 1.85 A resolution in a monoclinic crystal form (R factor = 16.1%, R(free) = 22.0%). Comparison of P. epiclitum (recombinant versus wild-type ferric Hb) structures in the two crystal forms shows structural differences in the haem proximal and distal sites which have not been reported for other known haemoglobin structures previously.
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{{ABSTRACT_PUBMED_11914507}}


==About this Structure==
==About this Structure==
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[[Category: Pesce, A.]]
[[Category: Pesce, A.]]
[[Category: Hemoglobin]]
[[Category: Hemoglobin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 10:16:38 2008''

Revision as of 07:16, 2 July 2008

File:1kfr.png

Template:STRUCTURE 1kfr

Structural plasticity in the eight-helix fold of a trematode hemoglobin

Template:ABSTRACT PUBMED 11914507

About this Structure

1KFR is a Single protein structure of sequence from Paramphistomum epiclitum. Full crystallographic information is available from OCA.

Reference

Structural plasticity in the eight-helix fold of a trematode haemoglobin., Milani M, Pesce A, Dewilde S, Ascenzi P, Moens L, Bolognesi M, Acta Crystallogr D Biol Crystallogr. 2002 Apr;58(Pt 4):719-22. Epub 2002, Mar 22. PMID:11914507

Page seeded by OCA on Wed Jul 2 10:16:38 2008

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