1ryx: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-{{Seed}}
-[[Image:1ryx.png|left|200px]]
-<!--
+==Crystal structure of hen serum transferrin in apo- form==
-The line below this paragraph, containing "STRUCTURE_1ryx", creates the "Structure Box" on the page.
+<StructureSection load='1ryx' size='340' side='right'caption='[[1ryx]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1ryx]] 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=1RYX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RYX FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.5&#8491;</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=1ryx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ryx OCA], [https://pdbe.org/1ryx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ryx RCSB], [https://www.ebi.ac.uk/pdbsum/1ryx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ryx ProSAT]</span></td></tr>
-{{STRUCTURE_1ryx|  PDB=1ryx  |  SCENE=  }}
+</table>
+== 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.
+== 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/ry/1ryx_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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/main_output.php?pdb_ID=1ryx ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The iron binding and release of serum transferrin are pH-dependent and accompanied by a conformational change between the iron-bound (holo-) and iron-free (apo-) forms. We have determined the crystal structure of apo-hen serum transferrin (hAST) at 3.5A resolution, which is the first reported structure to date of any full molecule of an apo-serum transferrin and studied its pH-dependent iron release by UV-vis absorption and near UV-CD spectroscopy. The crystal structure of hAST shows that both the lobes adopt an open conformation and the relative orientations of the domains are different from those of apo-human serum transferrin and human apolactoferrin but similar to that of hen apo-ovotransferrin. Spectroscopic analysis reveals that in hen serum transferrin, release of the first iron starts at a pH approximately 6.5 and continues over a broad pH range (6.5-5.2). The complete release of the iron, however, occurs at pH approximately 4.0. The near UV-CD spectra show alterations in the microenvironment of the aromatic residues surrounding the iron-binding sites.
-===Crystal structure of hen serum transferrin in apo- form===
+Tertiary structural changes associated with iron binding and release in hen serum transferrin: a crystallographic and spectroscopic study.,Thakurta PG, Choudhury D, Dasgupta R, Dattagupta JK Biochem Biophys Res Commun. 2004 Apr 16;316(4):1124-31. PMID:15044101<ref>PMID:15044101</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1ryx" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_15044101}}, adds the Publication Abstract to the page
+*[[Transferrin 3D structures|Transferrin 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 15044101 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_15044101}}
+__TOC__
+</StructureSection>
-==About this Structure==
-RYX is a 1 chain structure of 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=1RYX OCA].
-==Reference==
-<ref group="xtra">PMID:15044101</ref><references group="xtra"/>
 [[Category: Gallus gallus]]
-[[Category: Choudhury, D.]]
+[[Category: Large Structures]]
-[[Category: Dasgupta, R.]]
+[[Category: Choudhury D]]
-[[Category: Dattagupta, J K.]]
+[[Category: Dasgupta R]]
-[[Category: Thakurta, P G.]]
+[[Category: Dattagupta JK]]
-[[Category: Apo- form]]
+[[Category: Thakurta PG]]
-[[Category: Domain orientation]]
-[[Category: Hen serum transferrin]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 09:47:13 2009''