8c7p: Difference between revisions
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==Tagless BtuM in complex with cyanocobalamin== | |||
<StructureSection load='8c7p' size='340' side='right'caption='[[8c7p]], [[Resolution|resolution]] 3.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8c7p]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thiobacillus_denitrificans_ATCC_25259 Thiobacillus denitrificans ATCC 25259]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8C7P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8C7P 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]] 3Å</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=8c7p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8c7p OCA], [https://pdbe.org/8c7p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8c7p RCSB], [https://www.ebi.ac.uk/pdbsum/8c7p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8c7p ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q3SFD8_THIDA Q3SFD8_THIDA] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
BtuM is a bacterial cobalamin transporter that binds the transported substrate in the base-off state, with a cysteine residue providing the alpha-axial coordination of the central cobalt ion via a sulfur-cobalt bond. Binding leads to decyanation of cobalamin variants with a cyano group as the beta-axial ligand. Here, we report the crystal structures of untagged BtuM bound to two variants of cobalamin, hydroxycobalamin and cyanocobalamin, and unveil the native residue responsible for the beta-axial coordination, His28. This coordination had previously been obscured by non-native histidines of His-tagged BtuM. A model in which BtuM initially binds cobinamide reversibly with low affinity (K(D) = 4.0 muM), followed by the formation of a covalent bond (rate constant of 0.163 s(-1)), fits the kinetics data of substrate binding and decyanation of the cobalamin precursor cobinamide by BtuM. The covalent binding mode suggests a mechanism not used by any other transport protein. | |||
Cobalamin decyanation by the membrane transporter BtuM.,Martinez Felices JM, Barreto YB, Thangaratnarajah C, Whittaker JJ, Alencar AM, Guskov A, Slotboom DJ Structure. 2024 Aug 8;32(8):1165-1173.e3. doi: 10.1016/j.str.2024.04.014. Epub , 2024 May 10. PMID:38733996<ref>PMID:38733996</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 8c7p" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Thiobacillus denitrificans ATCC 25259]] | |||
[[Category: Martinez-Felices JM]] | |||
[[Category: Slotboom DJ]] | |||
Latest revision as of 19:35, 8 September 2026
Tagless BtuM in complex with cyanocobalamin
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