1kfr

From Proteopedia

(Difference between revisions)
Jump to: navigation, search

OCA (Talk | contribs)
(New page: 200px<br /> <applet load="1kfr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kfr, resolution 1.85&Aring;" /> '''Structural plastici...)
Next diff →

Revision as of 11:05, 8 November 2007

Image:1kfr.gif

1kfr, resolution 1.85Å

Drag the structure with the mouse to rotate

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

Overview

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.

About this Structure

1KFR is a Single protein structure of sequence from Paramphistomum epiclitum with SO4 and HEM as ligands. 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 Thu Nov 8 13:11:15 2007

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1kfr"
Personal tools