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6G3R

Structure of tellurium-centred Anderson-Evans polyoxotungstate (TEW) bound to the nucleotide binding domain of HSP70. Structure one of two TEW-HSP70 structures deposited.

Summary for 6G3R
Entry DOI10.2210/pdb6g3r/pdb
DescriptorHeat shock 70 kDa protein 1A, ADENOSINE-5'-DIPHOSPHATE, 6-tungstotellurate(VI), ... (7 entities in total)
Functional Keywordsatpase domain, chaperone
Biological sourceHomo sapiens (Human)
Total number of polymer chains1
Total formula weight44089.47
Authors
Mac Sweeney, A.,Chambovey, A.,Wicki, M.,Mueller, M.,Artico, N.,Lange, R.,Bijelic, A.,Breibeck, J.,Rompel, A. (deposition date: 2018-03-26, release date: 2018-10-17, Last modification date: 2024-05-08)
Primary citationMac Sweeney, A.,Chambovey, A.,Wicki, M.,Muller, M.,Artico, N.,Lange, R.,Bijelic, A.,Breibeck, J.,Rompel, A.
The crystallization additive hexatungstotellurate promotes the crystallization of the HSP70 nucleotide binding domain into two different crystal forms.
PLoS ONE, 13:e0199639-e0199639, 2018
Cited by
PubMed Abstract: The use of the tellurium-centered Anderson-Evans polyoxotungstate [TeW6O24]6- (TEW) as a crystallization additive has been described. Here, we present the use of TEW as an additive in the crystallization screening of the nucleotide binding domain (NBD) of HSP70. Crystallization screening of the HSP70 NBD in the absence of TEW using a standard commercial screen resulted in a single crystal form. An identical crystallization screen of the HSP70 NBD in the presence of TEW resulted in both the "TEW free" crystal form and an additional crystal form with a different crystal packing. TEW binding was observed in both crystal forms, either as a well-defined molecule or in overlapping alternate positions suggesting translational disorder. The structures were solved by both molecular replacement and single wavelength anomalous diffraction (SAD) using the anomalous signal of a single bound molecule of TEW. This study adds one more example of TEW binding to a protein and influencing its crystallization behavior.
PubMed: 29949628
DOI: 10.1371/journal.pone.0199639
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.4 Å)
Structure validation

231029

数据于2025-02-05公开中

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