3a8e: Difference between revisions
New page: '''Unreleased structure''' The entry 3a8e is ON HOLD Authors: Hu, S.Q., Tajima, K., Zhou, Y., Yao, M., Tanaka, I. Description: Crystal structure of C-His tagged AxCesD protein complexe... |
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The | ==The structure of AxCesD octamer complexed with cellopentaose== | ||
<StructureSection load='3a8e' size='340' side='right'caption='[[3a8e]], [[Resolution|resolution]] 3.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3a8e]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Komagataeibacter_xylinus Komagataeibacter xylinus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A8E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3A8E FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=PRD_900016:beta-cellopentaose'>PRD_900016</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=3a8e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a8e OCA], [https://pdbe.org/3a8e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3a8e RCSB], [https://www.ebi.ac.uk/pdbsum/3a8e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3a8e ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/ACSD_KOMXY ACSD_KOMXY] May have a major role in the perfection of crystallization, involved either in the pore structure itself or in the organization of the pores within the linear array of terminal synthesizing complexes (TCs). | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a8/3a8e_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</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=3a8e ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The cellulose synthesizing terminal complex consisting of subunits A, B, C, and D in Acetobacter xylinum spans the outer and inner cell membranes to synthesize and extrude glucan chains, which are assembled into subelementary fibrils and further into a ribbon. We determined the structures of subunit D (AxCeSD/AxBcsD) with both N- and C-terminal His(6) tags, and in complex with cellopentaose. The structure of AxCeSD shows an exquisite cylinder shape (height: approximately 65 A, outer diameter: approximately 90 A, and inner diameter: approximately 25 A) with a right-hand twisted dimer interface on the cylinder wall, formed by octamer as a functional unit. All N termini of the octamer are positioned inside the AxCeSD cylinder and create four passageways. The location of cellopentaoses in the complex structure suggests that four glucan chains are extruded individually through their own passageway along the dimer interface in a twisted manner. The complex structure also shows that the N-terminal loop, especially residue Lys6, seems to be important for cellulose production, as confirmed by in vivo assay using mutant cells with axcesD gene disruption and N-terminus truncation. Taking all results together, a model of the bacterial terminal complex is discussed. | |||
Structure of bacterial cellulose synthase subunit D octamer with four inner passageways.,Hu SQ, Gao YG, Tajima K, Sunagawa N, Zhou Y, Kawano S, Fujiwara T, Yoda T, Shimura D, Satoh Y, Munekata M, Tanaka I, Yao M Proc Natl Acad Sci U S A. 2010 Oct 19;107(42):17957-61. Epub 2010 Oct 4. PMID:20921370<ref>PMID:20921370</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3a8e" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Komagataeibacter xylinus]] | |||
[[Category: Large Structures]] | |||
[[Category: Hu SQ]] | |||
[[Category: Tajima K]] | |||
[[Category: Tanaka I]] | |||
[[Category: Yao M]] | |||
[[Category: Zhou Y]] | |||
Latest revision as of 17:15, 1 November 2023
The structure of AxCesD octamer complexed with cellopentaoseThe structure of AxCesD octamer complexed with cellopentaose
Structural highlights
FunctionACSD_KOMXY May have a major role in the perfection of crystallization, involved either in the pore structure itself or in the organization of the pores within the linear array of terminal synthesizing complexes (TCs). 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 PubMedThe cellulose synthesizing terminal complex consisting of subunits A, B, C, and D in Acetobacter xylinum spans the outer and inner cell membranes to synthesize and extrude glucan chains, which are assembled into subelementary fibrils and further into a ribbon. We determined the structures of subunit D (AxCeSD/AxBcsD) with both N- and C-terminal His(6) tags, and in complex with cellopentaose. The structure of AxCeSD shows an exquisite cylinder shape (height: approximately 65 A, outer diameter: approximately 90 A, and inner diameter: approximately 25 A) with a right-hand twisted dimer interface on the cylinder wall, formed by octamer as a functional unit. All N termini of the octamer are positioned inside the AxCeSD cylinder and create four passageways. The location of cellopentaoses in the complex structure suggests that four glucan chains are extruded individually through their own passageway along the dimer interface in a twisted manner. The complex structure also shows that the N-terminal loop, especially residue Lys6, seems to be important for cellulose production, as confirmed by in vivo assay using mutant cells with axcesD gene disruption and N-terminus truncation. Taking all results together, a model of the bacterial terminal complex is discussed. Structure of bacterial cellulose synthase subunit D octamer with four inner passageways.,Hu SQ, Gao YG, Tajima K, Sunagawa N, Zhou Y, Kawano S, Fujiwara T, Yoda T, Shimura D, Satoh Y, Munekata M, Tanaka I, Yao M Proc Natl Acad Sci U S A. 2010 Oct 19;107(42):17957-61. Epub 2010 Oct 4. PMID:20921370[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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