1dtg

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[[Image:1dtg.gif|left|200px]]<br /><applet load="1dtg" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1dtg.gif|left|200px]]
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caption="1dtg, resolution 2.4&Aring;" />
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'''HUMAN TRANSFERRIN N-LOBE MUTANT H249E'''<br />
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{{Structure
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|PDB= 1dtg |SIZE=350|CAPTION= <scene name='initialview01'>1dtg</scene>, resolution 2.4&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene> and <scene name='pdbligand=CO3:CARBONATE ION'>CO3</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''HUMAN TRANSFERRIN N-LOBE MUTANT H249E'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1DTG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] 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=1DTG OCA].
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1DTG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DTG OCA].
==Reference==
==Reference==
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Mutation of the iron ligand His 249 to Glu in the N-lobe of human transferrin abolishes the dilysine "trigger" but does not significantly affect iron release., MacGillivray RT, Bewley MC, Smith CA, He QY, Mason AB, Woodworth RC, Baker EN, Biochemistry. 2000 Feb 15;39(6):1211-6. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10684598 10684598]
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Mutation of the iron ligand His 249 to Glu in the N-lobe of human transferrin abolishes the dilysine "trigger" but does not significantly affect iron release., MacGillivray RT, Bewley MC, Smith CA, He QY, Mason AB, Woodworth RC, Baker EN, Biochemistry. 2000 Feb 15;39(6):1211-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10684598 10684598]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: signal]]
[[Category: signal]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:20:14 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:44:00 2008''

Revision as of 08:44, 20 March 2008

Image:1dtg.gif


PDB ID 1dtg

Drag the structure with the mouse to rotate
, resolution 2.4Å
Ligands: and
Coordinates: save as pdb, mmCIF, xml



HUMAN TRANSFERRIN N-LOBE MUTANT H249E


Contents

Overview

Serum transferrin is the major iron transport protein in humans. Its function depends on its ability to bind iron with very high affinity, yet to release this bound iron at the lower intracellular pH. Possible explanations for the release of iron from transferrin at low pH include protonation of a histidine ligand and the existence of a pH-sensitive "trigger" involving a hydrogen-bonded pair of lysines in the N-lobe of transferrin. We have determined the crystal structure of the His249Glu mutant of the N-lobe half-molecule of human transferrin and compared its iron-binding properties with those of the wild-type protein and other mutants. The crystal structure, determined at 2.4 A resolution (R-factor 19.8%, R(free) 29.4%), shows that Glu 249 is directly bound to iron, in place of the His ligand, and that a local movement of Lys 296 has broken the dilysine interaction. Despite the loss of this potentially pH-sensitive interaction, the H249E mutant is only slightly more acid-stable than wild-type and releases iron slightly faster. We conclude that the loss of the dilysine interaction does make the protein more acid stable but that this is counterbalanced by the replacement of a neutral ligand (His) by a negatively charged one (Glu), thus disrupting the electroneutrality of the binding site.

Disease

Known diseases associated with this structure: Atransferrinemia OMIM:[190000], Iron deficiency anemia, susceptibility to OMIM:[190000]

About this Structure

1DTG is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Mutation of the iron ligand His 249 to Glu in the N-lobe of human transferrin abolishes the dilysine "trigger" but does not significantly affect iron release., MacGillivray RT, Bewley MC, Smith CA, He QY, Mason AB, Woodworth RC, Baker EN, Biochemistry. 2000 Feb 15;39(6):1211-6. PMID:10684598

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