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6x8z

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Current revision

Crystal structure of N-truncated human B12 chaperone CblD(C262S)-thiolato-cob(III)alamin complex (108-296)

Structural highlights

6x8z is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.5Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

MMAD_HUMAN Methylcobalamin deficiency type cblDv1;Methylmalonic acidemia with homocystinuria, type cblD;Vitamin B12-responsive methylmalonic acidemia, type cblDv2. The disease is caused by mutations affecting the gene represented in this entry.

Function

MMAD_HUMAN Involved in cobalamin metabolism.^[1]

Publication Abstract from PubMed

The CblC and CblD chaperones are involved in early steps in the cobalamin trafficking pathway. Cobalamin derivatives entering the cytoplasm are converted by CblC to a common cob(II)alamin intermediate via glutathione-dependent alkyltransferase or reductive elimination activities. Cob(II)alamin is subsequently converted to one of two biologically active alkylcobalamins by downstream chaperones. The function of CblD has been elusive although it is known to form a complex with CblC under certain conditions. Here, we report that CblD provides a sulfur ligand to cob(II)alamin bound to CblC, forming an interprotein coordination complex that rapidly oxidizes to thiolato-cob(III)alamin. Cysteine scanning mutagenesis and EPR spectroscopy identified Cys-261 on CblD as the sulfur donor. The unusual interprotein Co-S bond was characterized by X-ray absorption spectroscopy and visualized in the crystal structure of the human CblD thiolato-cob(III)alamin complex. Our study provides insights into how cobalamin coordination chemistry could be utilized for cofactor translocation in the trafficking pathway.

An Interprotein Co-S Coordination Complex in the B12-Trafficking Pathway.,Li Z, Mascarenhas R, Twahir UT, Kallon A, Deb A, Yaw M, Penner-Hahn J, Koutmos M, Warncke K, Banerjee R J Am Chem Soc. 2020 Sep 14. doi: 10.1021/jacs.0c06590. PMID:32871076^[2]

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

References

↑ Coelho D, Suormala T, Stucki M, Lerner-Ellis JP, Rosenblatt DS, Newbold RF, Baumgartner MR, Fowler B. Gene identification for the cblD defect of vitamin B12 metabolism. N Engl J Med. 2008 Apr 3;358(14):1454-64. doi: 10.1056/NEJMoa072200. PMID:18385497 doi:http://dx.doi.org/10.1056/NEJMoa072200
↑ Li Z, Mascarenhas R, Twahir UT, Kallon A, Deb A, Yaw M, Penner-Hahn J, Koutmos M, Warncke K, Banerjee R. An Interprotein Co-S Coordination Complex in the B12-Trafficking Pathway. J Am Chem Soc. 2020 Sep 14. doi: 10.1021/jacs.0c06590. PMID:32871076 doi:http://dx.doi.org/10.1021/jacs.0c06590

1 Structural highlights
2 Disease
3 Function
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6x8z"

@@ Line 3: / Line 3: @@
 <StructureSection load='6x8z' size='340' side='right'caption='[[6x8z]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6x8z]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6X8Z OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6X8Z FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6x8z]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6X8Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6X8Z FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=B12:COBALAMIN'>B12</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]] 2.5&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MMADHC, C2orf25, CL25022, HSPC161, My011 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=B12:COBALAMIN'>B12</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6x8z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6x8z OCA], [http://pdbe.org/6x8z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6x8z RCSB], [http://www.ebi.ac.uk/pdbsum/6x8z PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6x8z 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=6x8z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6x8z OCA], [https://pdbe.org/6x8z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6x8z RCSB], [https://www.ebi.ac.uk/pdbsum/6x8z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6x8z ProSAT]</span></td></tr>
 </table>
 == Disease ==
-[[http://www.uniprot.org/uniprot/MMAD_HUMAN MMAD_HUMAN]] Methylcobalamin deficiency type cblDv1;Methylmalonic acidemia with homocystinuria, type cblD;Vitamin B12-responsive methylmalonic acidemia, type cblDv2. The disease is caused by mutations affecting the gene represented in this entry.
+[https://www.uniprot.org/uniprot/MMAD_HUMAN MMAD_HUMAN] Methylcobalamin deficiency type cblDv1;Methylmalonic acidemia with homocystinuria, type cblD;Vitamin B12-responsive methylmalonic acidemia, type cblDv2. The disease is caused by mutations affecting the gene represented in this entry.
 == Function ==
-[[http://www.uniprot.org/uniprot/MMAD_HUMAN MMAD_HUMAN]] Involved in cobalamin metabolism.<ref>PMID:18385497</ref>
+[https://www.uniprot.org/uniprot/MMAD_HUMAN MMAD_HUMAN] Involved in cobalamin metabolism.<ref>PMID:18385497</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 25: / Line 25: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Banerjee, R]]
+[[Category: Banerjee R]]
-[[Category: Koutmos, M]]
+[[Category: Koutmos M]]
-[[Category: Li, Z]]
+[[Category: Li Z]]
-[[Category: Mascarenhas, R]]
+[[Category: Mascarenhas R]]
-[[Category: Chaperone]]
-[[Category: Cobalamin]]
-[[Category: Oxidoreductase]]
-[[Category: Vitamin b12]]

6x8z

From Proteopedia

Current revision

Crystal structure of N-truncated human B12 chaperone CblD(C262S)-thiolato-cob(III)alamin complex (108-296)

Structural highlights

Disease

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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