This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

3l1m

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 12:31, 13 October 2021

Crystal Structure of a Ni-directed Dimer of Cytochrome cb562 with a Quinolate-Histidine Hybrid Coordination Motif

Structural highlights

3l1m is a 1 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Related:	256b, 2bc5, 3foo
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[C562_ECOLX] Electron-transport protein of unknown function.

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

Protein homodimerization is the simplest form of oligomerization that is frequently utilized for the construction of functional biological assemblies and the regulation of cellular pathways. Despite its simplicity, dimerization still poses an enormous challenge for protein engineering and chemical maniupulation, owing to the large molecular surfaces involved in this process. We report here the construction of a hybrid coordination motif-consisting of a natural (His) and a non-natural ligand (quinolate)-on the alpha-helical surface of cytochrome cb(562), which (a) simultaneously binds divalent metals with high affinity, (b) leads to a metal-induced increase in global protein stability, and importantly, (c) enables the formation of a discrete protein dimer, whose shape is dictated by the inner-sphere metal coordination geometry and closely approximates that of the DNA-binding domains of bZIP family transcription factors.

Controlled Protein Dimerization through Hybrid Coordination Motifs.,Radford RJ, Nguyen PC, Ditri TB, Figueroa JS, Tezcan FA Inorg Chem. 2010 May 3;49(9):4362-9. PMID:20377257^[1]

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

References

↑ Radford RJ, Nguyen PC, Ditri TB, Figueroa JS, Tezcan FA. Controlled Protein Dimerization through Hybrid Coordination Motifs. Inorg Chem. 2010 May 3;49(9):4362-9. PMID:20377257 doi:10.1021/ic100534y

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3l1m"

@@ Line 3: / Line 3: @@
 <StructureSection load='3l1m' size='340' side='right'caption='[[3l1m]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3l1m]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3L1M OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3L1M FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3l1m]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3L1M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3L1M FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=HQI:N-(8-HYDROXYQUINOLIN-5-YL)ACETAMIDE'>HQI</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[256b|256b]], [[2bc5|2bc5]], [[3foo|3foo]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[256b|256b]], [[2bc5|2bc5]], [[3foo|3foo]]</div></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=3l1m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l1m OCA], [http://pdbe.org/3l1m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3l1m RCSB], [http://www.ebi.ac.uk/pdbsum/3l1m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3l1m 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=3l1m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l1m OCA], [https://pdbe.org/3l1m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3l1m RCSB], [https://www.ebi.ac.uk/pdbsum/3l1m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3l1m ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/C562_ECOLX C562_ECOLX]] Electron-transport protein of unknown function.
+[[https://www.uniprot.org/uniprot/C562_ECOLX C562_ECOLX]] Electron-transport protein of unknown function.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

3l1m

From Proteopedia

Revision as of 12:31, 13 October 2021

Crystal Structure of a Ni-directed Dimer of Cytochrome cb562 with a Quinolate-Histidine Hybrid Coordination Motif

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox