1ce2

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[[Image:1ce2.gif|left|200px]]
[[Image:1ce2.gif|left|200px]]
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{{Structure
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|PDB= 1ce2 |SIZE=350|CAPTION= <scene name='initialview01'>1ce2</scene>, resolution 2.5&Aring;
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The line below this paragraph, containing "STRUCTURE_1ce2", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>
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{{STRUCTURE_1ce2| PDB=1ce2 | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ce2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ce2 OCA], [http://www.ebi.ac.uk/pdbsum/1ce2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ce2 RCSB]</span>
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}}
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'''STRUCTURE OF DIFERRIC BUFFALO LACTOFERRIN AT 2.5A RESOLUTION'''
'''STRUCTURE OF DIFERRIC BUFFALO LACTOFERRIN AT 2.5A RESOLUTION'''
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[[Category: Srinivasan, A.]]
[[Category: Srinivasan, A.]]
[[Category: Yadav, S.]]
[[Category: Yadav, S.]]
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[[Category: antibacterial]]
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[[Category: Antibacterial]]
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[[Category: iron binding protein]]
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[[Category: Iron binding protein]]
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[[Category: lactoferrin]]
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[[Category: Lactoferrin]]
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[[Category: room temperature]]
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[[Category: Room temperature]]
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[[Category: structure]]
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[[Category: Structure]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:37:34 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:19:47 2008''
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Revision as of 09:37, 2 May 2008

Image:1ce2.gif

Template:STRUCTURE 1ce2

STRUCTURE OF DIFERRIC BUFFALO LACTOFERRIN AT 2.5A RESOLUTION


Overview

The structure of buffalo lactoferrin has been determined at 303 K. The crystals belong to orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 77.5, b = 91.0, c = 131.5 A and Z = 4. The structure has been refined to an R factor of 0.187. The overall structure of the protein is similar to its structure determined at 277 K in a different crystal form. However, the lobe orientations in the two structures differ by 9.0 degrees, suggesting significant inter-lobe flexibility in this family of proteins. The inter-lobe interactions are predominantly hydrophobic and could act as a cushion for a change in orientation under the influence of external conditions. On the other hand, the domain arrangements are found to be similar in 277 and 303 K crystal structures, with orientations differing by 1.5 and 1.0 degrees in the N and C lobes, respectively. The results of these investigations suggest that the increase in temperature helps in the production of better quality crystals.

About this Structure

1CE2 is a Single protein structure of sequence from Bubalus bubalis. Full crystallographic information is available from OCA.

Reference

Structure of buffalo lactoferrin at 2.5 A resolution using crystals grown at 303 K shows different orientations of the N and C lobes., Karthikeyan S, Paramasivam M, Yadav S, Srinivasan A, Singh TP, Acta Crystallogr D Biol Crystallogr. 1999 Nov;55(Pt 11):1805-13. PMID:10531476 Page seeded by OCA on Fri May 2 12:37:34 2008

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