1ovt

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(Difference between revisions)

Revision as of 09:22, 8 September 2021

REFINED CRYSTALLOGRAPHIC STRUCTURE OF HEN OVOTRANSFERRIN AT 2.4 ANGSTROMS RESOLUTION

Structural highlights

1ovt is a 1 chain structure with sequence from Gallus gallus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[TRFE_CHICK] Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. Responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. There are two forms of hen transferrin, ovotransferrin, found in the ovoducts and, serum transferrin, secreted by the liver. Serum transferrin may also have a role in stimulating cell proliferation and is regulated by iron levels. Ovotransferrin has a bacteriostatic function and, is not controlled by iron levels.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The three-dimensional structure of diferric hen ovotransferrin has been determined by X-ray crystallography at 2.4 A resolution. The structure was solved by molecular replacement, using the coordinates of diferric human lactoferrin as a search model. Several rounds of simulated annealing and restrained least-squares refinement have resulted in a model structure with an R-factor of 0.171 for the data between 11.0 and 2.4 A resolution. The model comprises 5284 protein atoms (residues 5 to 686), 2 Fe3+, 2 CO3(2)- and 132 water molecules. The overall structure of ovotransferrin is similar to those of human lactoferrin and rabbit serum transferrin, being folded into two homologous lobes, each containing two dissimilar domains with one Fe3+ and one CO3(2)- bound at a specific site in each interdomain cleft. However, the relative orientation of the two lobes, which may be related to the class specificity of transferrins to receptors, is different from either human lactoferrin or rabbit serum transferrin. The angle of the relative orientation in ovotransferrin is increased by 6.8 degrees and 15.7 degrees as compared with to those in rabbit serum transferrin and human lactoferrin, respectively. Interdomain Lys209-Lys301 and Gln541-Lys638 interactions are found near the metal binding site of each lobe. The interlobe interactions and their role in the stabilization of iron binding are discussed.

Crystal structure of diferric hen ovotransferrin at 2.4 A resolution.,Kurokawa H, Mikami B, Hirose M J Mol Biol. 1995 Nov 24;254(2):196-207. PMID:7490743^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Kurokawa H, Mikami B, Hirose M. Crystal structure of diferric hen ovotransferrin at 2.4 A resolution. J Mol Biol. 1995 Nov 24;254(2):196-207. PMID:7490743 doi:http://dx.doi.org/10.1006/jmbi.1995.0611

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ovt"

@@ Line 3: / Line 3: @@
 <StructureSection load='1ovt' size='340' side='right'caption='[[1ovt]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1ovt]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OVT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OVT FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1ovt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OVT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OVT FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ovt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ovt OCA], [http://pdbe.org/1ovt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ovt RCSB], [http://www.ebi.ac.uk/pdbsum/1ovt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ovt ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ovt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ovt OCA], [https://pdbe.org/1ovt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ovt RCSB], [https://www.ebi.ac.uk/pdbsum/1ovt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ovt ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/TRFE_CHICK TRFE_CHICK]] Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. Responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. There are two forms of hen transferrin, ovotransferrin, found in the ovoducts and, serum transferrin, secreted by the liver. Serum transferrin may also have a role in stimulating cell proliferation and is regulated by iron levels. Ovotransferrin has a bacteriostatic function and, is not controlled by iron levels.
+[[https://www.uniprot.org/uniprot/TRFE_CHICK TRFE_CHICK]] Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. Responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. There are two forms of hen transferrin, ovotransferrin, found in the ovoducts and, serum transferrin, secreted by the liver. Serum transferrin may also have a role in stimulating cell proliferation and is regulated by iron levels. Ovotransferrin has a bacteriostatic function and, is not controlled by iron levels.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 30: / Line 30: @@
 ==See Also==
-*[[Transferrin|Transferrin]]
+*[[Transferrin 3D structures|Transferrin 3D structures]]
 == References ==
 <references/>

1ovt

From Proteopedia

Revision as of 09:22, 8 September 2021

REFINED CRYSTALLOGRAPHIC STRUCTURE OF HEN OVOTRANSFERRIN AT 2.4 ANGSTROMS RESOLUTION

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

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