1ce2
From Proteopedia
(New page: 200px<br /><applet load="1ce2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ce2, resolution 2.5Å" /> '''STRUCTURE OF DIFERRIC...) |
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| - | [[Image:1ce2.gif|left|200px]]<br /><applet load="1ce2" size=" | + | [[Image:1ce2.gif|left|200px]]<br /><applet load="1ce2" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ce2, resolution 2.5Å" /> | caption="1ce2, resolution 2.5Å" /> | ||
'''STRUCTURE OF DIFERRIC BUFFALO LACTOFERRIN AT 2.5A RESOLUTION'''<br /> | '''STRUCTURE OF DIFERRIC BUFFALO LACTOFERRIN AT 2.5A RESOLUTION'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structure of buffalo lactoferrin has been determined at 303 K. The | + | 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== | ==About this Structure== | ||
| - | 1CE2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bubalus_bubalis Bubalus bubalis] with FE and CO3 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1CE2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bubalus_bubalis Bubalus bubalis] with <scene name='pdbligand=FE:'>FE</scene> and <scene name='pdbligand=CO3:'>CO3</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CE2 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Karthikeyan, S.]] | [[Category: Karthikeyan, S.]] | ||
[[Category: Paramasivam, M.]] | [[Category: Paramasivam, M.]] | ||
| - | [[Category: Singh, T | + | [[Category: Singh, T P.]] |
[[Category: Srinivasan, A.]] | [[Category: Srinivasan, A.]] | ||
[[Category: Yadav, S.]] | [[Category: Yadav, S.]] | ||
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[[Category: structure]] | [[Category: structure]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:05:05 2008'' |
Revision as of 10:05, 21 February 2008
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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 with and as ligands. 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
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