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.

4efr

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 16:23, 5 August 2016

Bombyx mori lipoprotein 7 (crystal form II) at 2.50 A resolution

Structural highlights

4efr is a 4 chain structure with sequence from Bombyx mori. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:
Related:	3pub, 4efp, 4efq
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Publication Abstract from PubMed

Three crystal structures of a lipoprotein (Bmlp7) of unknown function, a member of the 30 kDa lipoprotein family from mulberry silkworm (Bombyx mori L.) haemolymph, have been determined. The 1.33 A resolution structure is an excellent example of how a precise crystallographic study can contribute to protein identification. The correct sequence of this haemolymph-isolated protein was assigned thanks to superb-quality electron-density maps. Two unexpected cadmium cations were found in this crystal structure [Bmlp7-I(Cd)] and their presence may be connected to a detoxification mechanism in this insect. For a comparison of the metal-binding sites, the crystal structure of a platinum complex (Bmlp7-Pt) was also solved at 1.94 A resolution. The third (2.50 A resolution) structure, of the native protein harvested in a different season (Bmlp7-II), corresponds to a different polymorph with an altered pattern of intermolecular interactions and with a total absence of cadmium ions and highlights the possible involvement of Bmlp7 in the response to environmental pollution. The N-terminal domain of Bmlp7 has a fold resembling a clockwise spiral created by six helices and can be classified as a VHS domain. The C-terminal domain is folded as a beta-trefoil. The biological function of Bmlp7 is unknown, but its structural homology to sugar-binding proteins suggests that, in analogy to other 30 kDa haemolymph lipoproteins, it could play a role as an anti-apoptotic factor or function in the immune response of the insect to fungal infections.

High-resolution structure of Bombyx mori lipoprotein 7: crystallographic determination of the identity of the protein and its potential role in detoxification.,Pietrzyk AJ, Panjikar S, Bujacz A, Mueller-Dieckmann J, Lochynska M, Jaskolski M, Bujacz G Acta Crystallogr D Biol Crystallogr. 2012 Sep;68(Pt 9):1140-51. doi:, 10.1107/S0907444912021555. Epub 2012 Aug 18. PMID:22948915^[1]

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

References

↑ Pietrzyk AJ, Panjikar S, Bujacz A, Mueller-Dieckmann J, Lochynska M, Jaskolski M, Bujacz G. High-resolution structure of Bombyx mori lipoprotein 7: crystallographic determination of the identity of the protein and its potential role in detoxification. Acta Crystallogr D Biol Crystallogr. 2012 Sep;68(Pt 9):1140-51. doi:, 10.1107/S0907444912021555. Epub 2012 Aug 18. PMID:22948915 doi:http://dx.doi.org/10.1107/S0907444912021555

1 Structural highlights
2 Publication Abstract from PubMed
3 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4efr"

@@ Line 1: / Line 1: @@
 ==Bombyx mori lipoprotein 7 (crystal form II) at 2.50 A resolution==
 <StructureSection load='4efr' size='340' side='right' caption='[[4efr]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=0AF:7-HYDROXY-L-TRYPTOPHAN'>0AF</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3pub|3pub]], [[4efp|4efp]], [[4efq|4efq]]</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4efr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4efr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4efr RCSB], [http://www.ebi.ac.uk/pdbsum/4efr PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4efr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4efr OCA], [http://pdbe.org/4efr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4efr RCSB], [http://www.ebi.ac.uk/pdbsum/4efr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4efr ProSAT]</span></td></tr>
 </table>
 <div style="background-color:#fffaf0;">
@@ Line 16: / Line 17: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4efr" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

4efr

From Proteopedia

Revision as of 16:23, 5 August 2016

Bombyx mori lipoprotein 7 (crystal form II) at 2.50 A resolution

Structural highlights

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox