1l0q

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<StructureSection load='1l0q' size='340' side='right'caption='[[1l0q]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
<StructureSection load='1l0q' size='340' side='right'caption='[[1l0q]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1l0q]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanosarcina_mazei_s-6 Methanosarcina mazei s-6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L0Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1L0Q FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1l0q]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanosarcina_mazei_S-6 Methanosarcina mazei S-6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L0Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1L0Q FirstGlance]. <br>
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</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=YCM:S-(2-AMINO-2-OXOETHYL)-L-CYSTEINE'>YCM</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ijq|1ijq]], [[1b4r|1b4r]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=YCM:S-(2-AMINO-2-OXOETHYL)-L-CYSTEINE'>YCM</scene></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=1l0q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l0q OCA], [https://pdbe.org/1l0q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1l0q RCSB], [https://www.ebi.ac.uk/pdbsum/1l0q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1l0q 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=1l0q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l0q OCA], [https://pdbe.org/1l0q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1l0q RCSB], [https://www.ebi.ac.uk/pdbsum/1l0q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1l0q ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q50245_METMZ Q50245_METMZ]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1l0q ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1l0q ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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The surface layer of archaeobacteria protects cells from extreme environments and, in Methanosarcina, may regulate cell adhesion. We identify three domain types that account for the complete architecture of numerous Methanosarcina surface layer proteins (SLPs). We solve the crystal structure for two of these domains, which correspond to the two N-terminal domains of an M. mazei SLP. One domain displays a unique, highly symmetrical, seven-bladed beta propeller fold, and the other belongs to the polycystic kidney disease (PKD) superfamily fold. The third domain is predicted to adopt a beta helix fold. These domains have homologs in metazoan cell surface proteins, suggesting remarkable relationships between domains in archaeal SLPs and metazoan cell surface proteins.
 
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Archaeal surface layer proteins contain beta propeller, PKD, and beta helix domains and are related to metazoan cell surface proteins.,Jing H, Takagi J, Liu JH, Lindgren S, Zhang RG, Joachimiak A, Wang JH, Springer TA Structure. 2002 Oct;10(10):1453-64. PMID:12377130<ref>PMID:12377130</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 1l0q" style="background-color:#fffaf0;"></div>
 
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Methanosarcina mazei s-6]]
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[[Category: Methanosarcina mazei S-6]]
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[[Category: Jing, H]]
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[[Category: Jing H]]
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[[Category: Joachimiak, A]]
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[[Category: Joachimiak A]]
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[[Category: Lindgren, S]]
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[[Category: Lindgren S]]
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[[Category: Liu, J H]]
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[[Category: Liu J-H]]
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[[Category: Springer, T A]]
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[[Category: Springer TA]]
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[[Category: Takagi, J]]
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[[Category: Takagi J]]
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[[Category: Wang, J H]]
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[[Category: Wang J-H]]
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[[Category: Zhang, R G]]
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[[Category: Zhang R-G]]
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[[Category: 7-bladed beta-propeller]]
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[[Category: Pkd superfamily]]
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[[Category: Protein binding]]
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[[Category: S-layer]]
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[[Category: Slp]]
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[[Category: Surface layer protein]]
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Revision as of 08:05, 3 April 2024

Tandem YVTN beta-propeller and PKD domains from an archaeal surface layer protein

PDB ID 1l0q

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