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.

3u2h

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

Crystal structure of the C-terminal DUF1608 domain of the Methanosarcina acetivorans S-layer (MA0829) protein

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3u2h"

@@ Line 3: / Line 3: @@
 <StructureSection load='3u2h' size='340' side='right'caption='[[3u2h]], [[Resolution|resolution]] 2.36&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3u2h]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Metac Metac]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U2H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3U2H FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3u2h]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanosarcina_acetivorans_C2A Methanosarcina acetivorans C2A]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U2H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3U2H FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 2.36&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3u2g|3u2g]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MA0829, MA_0829 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=188937 METAC])</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=3u2h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u2h OCA], [https://pdbe.org/3u2h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3u2h RCSB], [https://www.ebi.ac.uk/pdbsum/3u2h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3u2h ProSAT]</span></td></tr>
 </table>
-<div style="background-color:#fffaf0;">
+== Function ==
-== Publication Abstract from PubMed ==
+[https://www.uniprot.org/uniprot/CSG_METAC CSG_METAC] S-layer protein. The S-layer is a paracrystalline mono-layered assembly of proteins which coat the surface of the cell.<ref>PMID:19228054</ref>
-Archaea have a self-assembling proteinaceous surface (S-) layer as the primary and outermost boundary of their cell envelopes. The S-layer maintains structural rigidity, protects the organism from adverse environmental elements, and yet provides access to all essential nutrients. We have determined the crystal structure of one of the two "homologous" tandem polypeptide repeats that comprise the Methanosarcina acetivorans S-layer protein and propose a high-resolution model for a microbial S-layer. The molecular features of our hexameric S-layer model recapitulate those visualized by medium resolution electron microscopy studies of microbial S-layers and greatly expand our molecular view of S-layer dimensions, porosity, and symmetry. The S-layer model reveals a negatively charged molecular sieve that presents both a charge and size barrier to restrict access to the cell periplasmic-like space. The beta-sandwich folds of the S-layer protein are structurally homologous to eukaryotic virus envelope proteins, suggesting that Archaea and viruses have arrived at a common solution for protective envelope structures. These results provide insight into the evolutionary origins of primitive cell envelope structures, of which the S-layer is considered to be among the most primitive: it also provides a platform for the development of self-assembling nanomaterials with diverse functional and structural properties.
-Structure of the surface layer of the methanogenic archaean Methanosarcina acetivorans.,Arbing MA, Chan S, Shin A, Phan T, Ahn CJ, Rohlin L, Gunsalus RP Proc Natl Acad Sci U S A. 2012 Jul 17;109(29):11812-7. Epub 2012 Jul 2. PMID:22753492<ref>PMID:22753492</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3u2h" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
@@ Line 23: / Line 15: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Metac]]
+[[Category: Methanosarcina acetivorans C2A]]
-[[Category: Ahn, C J]]
+[[Category: Ahn CJ]]
-[[Category: Arbing, M A]]
+[[Category: Arbing MA]]
-[[Category: Chan, S]]
+[[Category: Chan S]]
-[[Category: Gunsalus, R P]]
+[[Category: Gunsalus RP]]
-[[Category: Phan, T]]
+[[Category: Phan T]]
-[[Category: Rohlin, L]]
+[[Category: Rohlin L]]
-[[Category: Shin, A]]
+[[Category: Shin A]]
-[[Category: Cell envelop]]
-[[Category: Duf1608 domain]]
-[[Category: S-layer]]
-[[Category: Structural protein]]
-[[Category: Surface layer]]
-[[Category: Unknown function]]

3u2h

From Proteopedia

Current revision

Crystal structure of the C-terminal DUF1608 domain of the Methanosarcina acetivorans S-layer (MA0829) protein

Structural highlights

Function

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox