3byr: Difference between revisions

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<StructureSection load='3byr' size='340' side='right'caption='[[3byr]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='3byr' size='340' side='right'caption='[[3byr]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3byr]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BYR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BYR FirstGlance]. <br>
<table><tr><td colspan='2'>[[3byr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BYR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BYR FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 1.8&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3byp|3byp]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=3byr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3byr OCA], [https://pdbe.org/3byr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3byr RCSB], [https://www.ebi.ac.uk/pdbsum/3byr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3byr 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=3byr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3byr OCA], [https://pdbe.org/3byr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3byr RCSB], [https://www.ebi.ac.uk/pdbsum/3byr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3byr ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q8VLX7_THETH Q8VLX7_THETH]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=3byr 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=3byr ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The crystal structures of the cytoplasmic domain of the putative zinc transporter CzrB in the apo and zinc-bound forms reported herein are consistent with the protein functioning in vivo as a homodimer. NMR, X-ray scattering, and size-exclusion chromatography provide support for dimer formation. Full-length variants of CzrB in the apo and zinc-loaded states were generated by homology modeling with the Zn2+/H+ antiporter YiiP. The model suggests a way in which zinc binding to the cytoplasmic fragment creates a docking site to which a metallochaperone can bind for delivery and transport of its zinc cargo. Because the cytoplasmic domain may exist in the cell as an independent, soluble protein, a proposal is advanced that it functions as a metallochaperone and that it regulates the zinc-transporting activity of the full-length protein. The latter requires that zinc binding becomes uncoupled from the creation of a metallochaperone-docking site on CzrB.
Insights into the mode of action of a putative zinc transporter CzrB in Thermus thermophilus.,Cherezov V, Hofer N, Szebenyi DM, Kolaj O, Wall JG, Gillilan R, Srinivasan V, Jaroniec CP, Caffrey M Structure. 2008 Sep 10;16(9):1378-88. PMID:18786400<ref>PMID:18786400</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3byr" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Caffrey, M]]
[[Category: Thermus thermophilus]]
[[Category: Cherezov, V]]
[[Category: Caffrey M]]
[[Category: Srinivasan, V]]
[[Category: Cherezov V]]
[[Category: Szebenyi, D M.E]]
[[Category: Srinivasan V]]
[[Category: Membrane protein]]
[[Category: Szebenyi DME]]
[[Category: Transport protein]]
[[Category: Zinc transporter]]

Latest revision as of 12:31, 21 February 2024

Mode of Action of a Putative Zinc Transporter CzrB (Zn form)Mode of Action of a Putative Zinc Transporter CzrB (Zn form)

Structural highlights

3byr is a 1 chain structure with sequence from Thermus thermophilus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.8Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q8VLX7_THETH

Evolutionary Conservation

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

3byr, resolution 1.80Å

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

OCA
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