2zg9: Difference between revisions

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==Crystal Structure of Pd(allyl)/apo-H114AFr==
==Crystal Structure of Pd(allyl)/apo-H114AFr==
<StructureSection load='2zg9' size='340' side='right' caption='[[2zg9]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
<StructureSection load='2zg9' size='340' side='right' caption='[[2zg9]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2zg7|2zg7]], [[2zg8|2zg8]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2zg7|2zg7]], [[2zg8|2zg8]]</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FTL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9796 Equus caballus])</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FTL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9796 Equus caballus])</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=2zg9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zg9 OCA], [http://pdbe.org/2zg9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2zg9 RCSB], [http://www.ebi.ac.uk/pdbsum/2zg9 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=2zg9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zg9 OCA], [http://pdbe.org/2zg9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2zg9 RCSB], [http://www.ebi.ac.uk/pdbsum/2zg9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2zg9 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zg/2zg9_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zg/2zg9_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>

Revision as of 09:49, 18 October 2018

Crystal Structure of Pd(allyl)/apo-H114AFrCrystal Structure of Pd(allyl)/apo-H114AFr

Structural highlights

2zg9 is a 1 chain structure with sequence from Equus caballus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, , ,
Gene:FTL (Equus caballus)
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[FRIL_HORSE] Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation. Also plays a role in delivery of iron to cells. Mediates iron uptake in capsule cells of the developing kidney (By similarity).

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

We report the preparation of organometallic Pd(allyl) dinuclear complexes in protein cages of apo-Fr by reactions with [Pd(allyl)Cl]2 (allyl = eta3-C3H5). One of the dinuclear complexes is converted to a trinuclear complex by replacing a Pd-coordinated His residue to an Ala residue. These results suggest that multinuclear metal complexes with various coordination structures could be prepared by the deletion or introduction of His, Cys, and Glu at appropriate positions on protein surface.

Control of the coordination structure of organometallic palladium complexes in an apo-ferritin cage.,Abe S, Niemeyer J, Abe M, Takezawa Y, Ueno T, Hikage T, Erker G, Watanabe Y J Am Chem Soc. 2008 Aug 13;130(32):10512-4. Epub 2008 Jul 18. PMID:18636721[1]

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

See Also

References

  1. Abe S, Niemeyer J, Abe M, Takezawa Y, Ueno T, Hikage T, Erker G, Watanabe Y. Control of the coordination structure of organometallic palladium complexes in an apo-ferritin cage. J Am Chem Soc. 2008 Aug 13;130(32):10512-4. Epub 2008 Jul 18. PMID:18636721 doi:10.1021/ja802463a

2zg9, resolution 1.75Å

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