1iej - Revision history

OCA at 07:46, 3 April 2024

OCA — Wed, 03 Apr 2024 07:46:45 GMT

←Older revision		Revision as of 07:46, 3 April 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1iej]] 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=1IEJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IEJ FirstGlance]. <br>		<table><tr><td colspan='2'>[[1iej]] 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=1IEJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IEJ FirstGlance]. <br>
-	</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>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 1.65Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max-height~~: ~~3em;~~'>~~[[1nnt\|1nnt]]~~</~~div~~></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'>[https://proteopedia.org/fgij/fg.htm?mol=1iej FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iej OCA], [https://pdbe.org/1iej PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1iej RCSB], [https://www.ebi.ac.uk/pdbsum/1iej PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1iej 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=1iej FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iej OCA], [https://pdbe.org/1iej PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1iej RCSB], [https://www.ebi.ac.uk/pdbsum/1iej PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1iej ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[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.	+	[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 ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 20:		Line 20:
	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1iej ConSurf].		</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1iej ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	The crystal structure of holo hen ovotransferrin N-lobe refined at 1.65 A resolution has been obtained. The final model gave an R-factor of 0.173 in the resolution range between 10.0 and 1.65 A. The comparison of the structure with previous high-resolution apo and Fe(3+)-loaded, domain-opened intermediate structures provides new viewpoints on the domain closure mechanism upon Fe(3+) uptake in ovotransferrin N-lobe. Overall, conformational transition follows the common mechanism that has been first demonstrated for lactoferrin N-lobe; the domains 1 and 2 rotate 49.7 degrees as rigid bodies with a translation of 2.1 A around a screw-axis that passes through the two interdomain beta-strands (89-94 and 244-249). It is generally believed that the two strands display a hinge-like motion. Here, the latter strand indeed displays an ideal hinge nature: the segments 244-246 and 248-249 behave as a part of the rigid body of domain 2 and that of domain 1, respectively, and a sharp bend upon the domain closure is largely accounted for by the changes in the torsion angles phi and psi of Val247. We find, however, that the mode of the conformational change in the first beta-strand is much more complex. Two of the five inter beta-strand hydrogen bonds undergo crucial exchanges: from Ser91-N...Val247-O and Thr89-O...Ala249-N in the open apo and intermediate structures into Tyr92-N...Val247-O and Thr90-O...Ala249-N in the closed holo structure. These exchanges, which may be triggered in the intermediate state by modulation in the topological relation between the Fe(3+)-ligated hinge residue Tyr92-OH and the anion anchor residues of helix 5, are accompanied by a large conformational change and extensive hydrogen bonding rearrangements in a long stretch of segment of Glu82 to Tyr92. Such structural transition would work as a driving force for the domain closure, which highlights a "door closer"-like role, in addition to the canonical-hinge role, for the interdomain polypeptide segment pair. As an alternative hinge that secures the correct domain motion by being placed on a significant distance from the beta-strand hinge, we point out the participation of the van der Waals contacts formed between domain 1 residue of Met331 and domain 2 residues of Trp125, Ile129 and Trp140.
-
-	Domain closure mechanism in transferrins: new viewpoints about the hinge structure and motion as deduced from high resolution crystal structures of ovotransferrin N-lobe.,Mizutani K, Mikami B, Hirose M J Mol Biol. 2001 Jun 15;309(4):937-47. PMID:11399070<ref>PMID:11399070</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1iej" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Transferrin 3D structures\|Transferrin 3D structures]]		*[[Transferrin 3D structures\|Transferrin 3D structures]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Gallus gallus]]		[[Category: Gallus gallus]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Hirose, M]]	+	[[Category: Hirose M]]
-	[[Category: Mikami, B]]	+	[[Category: Mikami B]]
-	[[Category: Mizutani, K]]	+	[[Category: Mizutani K]]
-	~~[[Category: Iron]]~~	+
-	~~[[Category: Metal binding protein]]~~	+
-	~~[[Category: Ovotransferrin]]~~	+
-	~~[[Category: Transferrin~~]]	+

OCA at 10:59, 4 August 2021

OCA — Wed, 04 Aug 2021 10:59:58 GMT

←Older revision		Revision as of 10:59, 4 August 2021
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	<StructureSection load='1iej' size='340' side='right'caption='[[1iej]], [[Resolution\|resolution]] 1.65Å' scene=''>		<StructureSection load='1iej' size='340' side='right'caption='[[1iej]], [[Resolution\|resolution]] 1.65Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1iej]] 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=1IEJ OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1IEJ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1iej]] 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=1IEJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IEJ 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='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1nnt\|1nnt]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1nnt\|1nnt]]</div></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=1iej FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iej OCA], [~~http~~://pdbe.org/1iej PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1iej RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1iej PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1iej 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=1iej FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iej OCA], [https://pdbe.org/1iej PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1iej RCSB], [https://www.ebi.ac.uk/pdbsum/1iej PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1iej ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== 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 ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 31:		Line 31:

	==See Also==		==See Also==
-	*[[Transferrin\|Transferrin]]	+	*[[Transferrin 3D structures\|Transferrin 3D structures]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 10:26, 30 October 2019

OCA — Wed, 30 Oct 2019 10:26:21 GMT

←Older revision		Revision as of 10:26, 30 October 2019
Line 1:		Line 1:

	==OVOTRANSFERRIN, N-TERMINAL LOBE, HOLO FORM, AT 1.65 A RESOLUTION==		==OVOTRANSFERRIN, N-TERMINAL LOBE, HOLO FORM, AT 1.65 A RESOLUTION==
-	<StructureSection load='1iej' size='340' side='right' caption='[[1iej]], [[Resolution\|resolution]] 1.65Å' scene=''>	+	<StructureSection load='1iej' size='340' side='right'caption='[[1iej]], [[Resolution\|resolution]] 1.65Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1iej]] 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=1IEJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IEJ FirstGlance]. <br>		<table><tr><td colspan='2'>[[1iej]] 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=1IEJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IEJ FirstGlance]. <br>
Line 29:		Line 29:
	</div>		</div>
	<div class="pdbe-citations 1iej" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1iej" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Transferrin\|Transferrin]]
	== References ==		== References ==
	<references/>		<references/>
Line 34:		Line 37:
	</StructureSection>		</StructureSection>
	[[Category: Gallus gallus]]		[[Category: Gallus gallus]]
		+	[[Category: Large Structures]]
	[[Category: Hirose, M]]		[[Category: Hirose, M]]
	[[Category: Mikami, B]]		[[Category: Mikami, B]]

OCA at 09:26, 10 January 2018

OCA — Wed, 10 Jan 2018 09:26:54 GMT

←Older revision		Revision as of 09:26, 10 January 2018
Line 1:		Line 1:
		+
	==OVOTRANSFERRIN, N-TERMINAL LOBE, HOLO FORM, AT 1.65 A RESOLUTION==		==OVOTRANSFERRIN, N-TERMINAL LOBE, HOLO FORM, AT 1.65 A RESOLUTION==
	<StructureSection load='1iej' size='340' side='right' caption='[[1iej]], [[Resolution\|resolution]] 1.65Å' scene=''>		<StructureSection load='1iej' size='340' side='right' caption='[[1iej]], [[Resolution\|resolution]] 1.65Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1iej]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Chick Chick~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IEJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IEJ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1iej]] 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=1IEJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IEJ 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"><scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1nnt\|1nnt]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1nnt\|1nnt]]</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=1iej FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iej OCA], [http://pdbe.org/1iej PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1iej RCSB], [http://www.ebi.ac.uk/pdbsum/1iej PDBsum]</span></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=1iej FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iej OCA], [http://pdbe.org/1iej PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1iej RCSB], [http://www.ebi.ac.uk/pdbsum/1iej PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1iej ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 13:		Line 14:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ie/1iej_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ie/1iej_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
Line 28:		Line 29:
	</div>		</div>
	<div class="pdbe-citations 1iej" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1iej" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Transferrin\|Transferrin]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Chick~~]]	+	[[Category: Gallus gallus]]
	[[Category: Hirose, M]]		[[Category: Hirose, M]]
	[[Category: Mikami, B]]		[[Category: Mikami, B]]

OCA at 09:29, 7 February 2016

OCA — Sun, 07 Feb 2016 09:29:12 GMT

←Older revision		Revision as of 09:29, 7 February 2016
Line 17:		Line 17:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1iej ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 00:03, 10 September 2015

OCA — Thu, 10 Sep 2015 00:03:44 GMT

←Older revision		Revision as of 00:03, 10 September 2015
Line 2:		Line 2:
	<StructureSection load='1iej' size='340' side='right' caption='[[1iej]], [[Resolution\|resolution]] 1.65Å' scene=''>		<StructureSection load='1iej' size='340' side='right' caption='[[1iej]], [[Resolution\|resolution]] 1.65Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1iej]] 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=1IEJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IEJ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1iej]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Chick Chick]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IEJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IEJ 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"><scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1nnt\|1nnt]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1nnt\|1nnt]]</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=1iej FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iej OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1iej RCSB], [http://www.ebi.ac.uk/pdbsum/1iej PDBsum]</span></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=1iej FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iej OCA], [http://pdbe.org/1iej PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1iej RCSB], [http://www.ebi.ac.uk/pdbsum/1iej PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 27:		Line 27:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 1iej" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 34:		Line 35:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Gallus gallus~~]]	+	[[Category: Chick]]
	[[Category: Hirose, M]]		[[Category: Hirose, M]]
	[[Category: Mikami, B]]		[[Category: Mikami, B]]

OCA at 14:03, 24 December 2014

OCA — Wed, 24 Dec 2014 14:03:14 GMT

←Older revision		Revision as of 14:03, 24 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1iej]] 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=1IEJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IEJ FirstGlance]. <br>		<table><tr><td colspan='2'>[[1iej]] 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=1IEJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IEJ FirstGlance]. <br>
-	</td></tr><tr><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><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>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1nnt\|1nnt]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1nnt\|1nnt]]</td></tr>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1iej FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iej OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1iej RCSB], [http://www.ebi.ac.uk/pdbsum/1iej PDBsum]</span></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=1iej FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iej OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1iej RCSB], [http://www.ebi.ac.uk/pdbsum/1iej PDBsum]</span></td></tr>
-	<table>	+	</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.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 33:		Line 35:
	</StructureSection>		</StructureSection>
	[[Category: Gallus gallus]]		[[Category: Gallus gallus]]
-	[[Category: Hirose, M.]]	+	[[Category: Hirose, M]]
-	[[Category: Mikami, B.]]	+	[[Category: Mikami, B]]
-	[[Category: Mizutani, K.]]	+	[[Category: Mizutani, K]]
	[[Category: Iron]]		[[Category: Iron]]
	[[Category: Metal binding protein]]		[[Category: Metal binding protein]]
	[[Category: Ovotransferrin]]		[[Category: Ovotransferrin]]
	[[Category: Transferrin]]		[[Category: Transferrin]]

OCA at 11:22, 28 September 2014

OCA — Sun, 28 Sep 2014 11:22:37 GMT

←Older revision		Revision as of 11:22, 28 September 2014
Line 1:		Line 1:
-	[[~~Image:~~1iej.~~png~~\|~~left~~\|200px]]	+	==OVOTRANSFERRIN, N-TERMINAL LOBE, HOLO FORM, AT 1.65 A RESOLUTION==
		+	<StructureSection load='1iej' size='340' side='right' caption='[[1iej]], [[Resolution\|resolution]] 1.65Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1iej]] 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=1IEJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IEJ FirstGlance]. <br>
		+	</td></tr><tr><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><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1nnt\|1nnt]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1iej FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iej OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1iej RCSB], [http://www.ebi.ac.uk/pdbsum/1iej PDBsum]</span></td></tr>
		+	<table>
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ie/1iej_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
		+	<text>to colour the structure by Evolutionary Conservation</text>
		+	</jmolCheckbox>
		+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The crystal structure of holo hen ovotransferrin N-lobe refined at 1.65 A resolution has been obtained. The final model gave an R-factor of 0.173 in the resolution range between 10.0 and 1.65 A. The comparison of the structure with previous high-resolution apo and Fe(3+)-loaded, domain-opened intermediate structures provides new viewpoints on the domain closure mechanism upon Fe(3+) uptake in ovotransferrin N-lobe. Overall, conformational transition follows the common mechanism that has been first demonstrated for lactoferrin N-lobe; the domains 1 and 2 rotate 49.7 degrees as rigid bodies with a translation of 2.1 A around a screw-axis that passes through the two interdomain beta-strands (89-94 and 244-249). It is generally believed that the two strands display a hinge-like motion. Here, the latter strand indeed displays an ideal hinge nature: the segments 244-246 and 248-249 behave as a part of the rigid body of domain 2 and that of domain 1, respectively, and a sharp bend upon the domain closure is largely accounted for by the changes in the torsion angles phi and psi of Val247. We find, however, that the mode of the conformational change in the first beta-strand is much more complex. Two of the five inter beta-strand hydrogen bonds undergo crucial exchanges: from Ser91-N...Val247-O and Thr89-O...Ala249-N in the open apo and intermediate structures into Tyr92-N...Val247-O and Thr90-O...Ala249-N in the closed holo structure. These exchanges, which may be triggered in the intermediate state by modulation in the topological relation between the Fe(3+)-ligated hinge residue Tyr92-OH and the anion anchor residues of helix 5, are accompanied by a large conformational change and extensive hydrogen bonding rearrangements in a long stretch of segment of Glu82 to Tyr92. Such structural transition would work as a driving force for the domain closure, which highlights a "door closer"-like role, in addition to the canonical-hinge role, for the interdomain polypeptide segment pair. As an alternative hinge that secures the correct domain motion by being placed on a significant distance from the beta-strand hinge, we point out the participation of the van der Waals contacts formed between domain 1 residue of Met331 and domain 2 residues of Trp125, Ile129 and Trp140.

-	~~{{STRUCTURE_1iej\| PDB=1iej \| SCENE= }}~~	+	Domain closure mechanism in transferrins: new viewpoints about the hinge structure and motion as deduced from high resolution crystal structures of ovotransferrin N-lobe.,Mizutani K, Mikami B, Hirose M J Mol Biol. 2001 Jun 15;309(4):937-47. PMID:11399070<ref>PMID:11399070</ref>

-	~~===OVOTRANSFERRIN~~, ~~N-TERMINAL LOBE, HOLO FORM, AT 1.65 A RESOLUTION===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_11399070}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[1iej]] 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=1IEJ OCA].~~	+

	==See Also==		==See Also==
	*[[Transferrin\|Transferrin]]		*[[Transferrin\|Transferrin]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:011399070<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Gallus gallus]]		[[Category: Gallus gallus]]
	[[Category: Hirose, M.]]		[[Category: Hirose, M.]]

OCA at 06:14, 20 October 2012

OCA — Sat, 20 Oct 2012 06:14:49 GMT

←Older revision		Revision as of 06:14, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[1iej]] is a 1 chain structure ~~of [[Transferrin]]~~ 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=1IEJ OCA].	+	[[1iej]] 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=1IEJ OCA].

	==See Also==		==See Also==

OCA: Protected "1iej" [edit=sysop:move=sysop]

OCA — Wed, 25 Jul 2012 12:34:51 GMT

Protected "1iej" [edit=sysop:move=sysop]

←Older revision

Revision as of 12:34, 25 July 2012