1lfi

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{{STRUCTURE_1lfi| PDB=1lfi | SCENE= }}
{{STRUCTURE_1lfi| PDB=1lfi | SCENE= }}
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'''METAL SUBSTITUTION IN TRANSFERRINS: THE CRYSTAL STRUCTURE OF HUMAN COPPER-LACTOFERRIN AT 2.1 ANGSTROMS RESOLUTION'''
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===METAL SUBSTITUTION IN TRANSFERRINS: THE CRYSTAL STRUCTURE OF HUMAN COPPER-LACTOFERRIN AT 2.1 ANGSTROMS RESOLUTION===
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==Overview==
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The structural consequences of binding a metal other than iron to a transferrin have been examined by crystallographic analysis of human copper-lactoferrin, Cu2Lf. X-ray diffraction data were collected from crystals of Cu2Lf, using a diffractometer, to 2.6-A resolution, and oscillation photography on a synchrotron source, to 2.1-A resolution. The structure was refined crystallographically, by restrained least-squares methods, starting with a model based on the isomorphous diferric structure from which the ligands, metal ions, anions, and solvent molecules had been deleted. The final model, comprising 5321 protein atoms (691 residues), 2 Cu2+ ions, 2 (bi)carbonate ions, and 308 solvent molecules has good stereochemistry (rms deviation of bond lengths from standard values of 0.018 A) and gives a crystallographic R value of 0.196 for 43,525 reflections in the range 7.5-2.1-A resolution. The copper coordination is different in the two binding sites. In the N-terminal site, the geometry is square pyramidal, with equatorial bonds to Asp 60, Tyr 192, His 253, and a monodentate anion and a longer apical bond to Tyr 92. In the C-terminal site, the geometry is distorted octahedral, with bonds to Asp 395, Tyr 435, Tyr 528, and His 597 and an asymmetrically bidentate anion. The protein structure is the same as for the diferric protein, Fe2Lf, demonstrating that the closure of the protein domains over the metal is the same in each case irrespective of whether Fe3+ or Cu2+ is bound and that copper could be transported and delivered to cells equally well as iron. The differences in metal coordination are achieved by small movements of the metal ion and anion within each binding site, which do not affect the protein structure.
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(as it appears on PubMed at http://www.pubmed.gov), where 1581307 is the PubMed ID number.
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{{ABSTRACT_PUBMED_1581307}}
==About this Structure==
==About this Structure==
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[[Category: Smith, C A.]]
[[Category: Smith, C A.]]
[[Category: Iron transport]]
[[Category: Iron transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:52:29 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 12:34:00 2008''

Revision as of 09:34, 27 July 2008

Image:1lfi.png

Template:STRUCTURE 1lfi

METAL SUBSTITUTION IN TRANSFERRINS: THE CRYSTAL STRUCTURE OF HUMAN COPPER-LACTOFERRIN AT 2.1 ANGSTROMS RESOLUTION

Template:ABSTRACT PUBMED 1581307

About this Structure

1LFI is a Single protein structure. Full crystallographic information is available from OCA.

Reference

Metal substitution in transferrins: the crystal structure of human copper-lactoferrin at 2.1-A resolution., Smith CA, Anderson BF, Baker HM, Baker EN, Biochemistry. 1992 May 12;31(18):4527-33. PMID:1581307

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