6uj6: Difference between revisions
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The | ==X-ray Crystal Structure of Chromium-transferrin with Synergistic Anion Malonate== | ||
<StructureSection load='6uj6' size='340' side='right'caption='[[6uj6]], [[Resolution|resolution]] 2.68Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6UJ6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6UJ6 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.68Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BCT:BICARBONATE+ION'>BCT</scene>, <scene name='pdbligand=CR:CHROMIUM+ION'>CR</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</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=6uj6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6uj6 OCA], [https://pdbe.org/6uj6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6uj6 RCSB], [https://www.ebi.ac.uk/pdbsum/6uj6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6uj6 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Transferrin, the Fe(III) transport protein in mammalian blood, has been suggested to also serve as a Cr(III) transporter and as part of a Cr(III) detoxification system; however, the structure of the metal-binding sites has never been fully elucidated with bound Cr(III). Chromium(III)-transferrin was crystallized in the presence of the synergistic anion malonate. In the crystals, the protein exists with a closed C-terminal lobe containing a Cr(III) ion and an open, unoccupied N-terminal lobe. The overall structure and the metal ion environments are extremely similar to those of Fe(III)- and Ti(IV)-containing transferrin crystallized under comparable conditions. The octahedral coordination about the Cr(III) is comprised of four ligands provided by the protein (two tyrosine residues, a histidine residue, and an aspartate residue) and a chelating malonate anion. This represents the first crystal structure of a Cr(III)-containing protein that binds Cr(III) as part of its physiological function. | |||
X-ray structure of chromium(III)-containing transferrin: First structure of a physiological Cr(III)-binding protein.,Petersen CM, Edwards KC, Gilbert NC, Vincent JB, Thompson MK J Inorg Biochem. 2020 Sep;210:111101. doi: 10.1016/j.jinorgbio.2020.111101. Epub , 2020 May 23. PMID:32650146<ref>PMID:32650146</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6uj6" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Transferrin 3D structures|Transferrin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Edwards KC]] | |||
[[Category: Gilbert NC]] | |||
[[Category: Petersen CM]] | |||
[[Category: Thompson MK]] | |||
[[Category: Vincent JB]] | |||
Latest revision as of 14:18, 30 October 2024
X-ray Crystal Structure of Chromium-transferrin with Synergistic Anion MalonateX-ray Crystal Structure of Chromium-transferrin with Synergistic Anion Malonate
Structural highlights
Publication Abstract from PubMedTransferrin, the Fe(III) transport protein in mammalian blood, has been suggested to also serve as a Cr(III) transporter and as part of a Cr(III) detoxification system; however, the structure of the metal-binding sites has never been fully elucidated with bound Cr(III). Chromium(III)-transferrin was crystallized in the presence of the synergistic anion malonate. In the crystals, the protein exists with a closed C-terminal lobe containing a Cr(III) ion and an open, unoccupied N-terminal lobe. The overall structure and the metal ion environments are extremely similar to those of Fe(III)- and Ti(IV)-containing transferrin crystallized under comparable conditions. The octahedral coordination about the Cr(III) is comprised of four ligands provided by the protein (two tyrosine residues, a histidine residue, and an aspartate residue) and a chelating malonate anion. This represents the first crystal structure of a Cr(III)-containing protein that binds Cr(III) as part of its physiological function. X-ray structure of chromium(III)-containing transferrin: First structure of a physiological Cr(III)-binding protein.,Petersen CM, Edwards KC, Gilbert NC, Vincent JB, Thompson MK J Inorg Biochem. 2020 Sep;210:111101. doi: 10.1016/j.jinorgbio.2020.111101. Epub , 2020 May 23. PMID:32650146[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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