3okg: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older edit
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
 
Line 3: Line 3:
<StructureSection load='3okg' size='340' side='right'caption='[[3okg]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
<StructureSection load='3okg' size='340' side='right'caption='[[3okg]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3okg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Cals4 Cals4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OKG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OKG FirstGlance]. <br>
<table><tr><td colspan='2'>[[3okg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Caldanaerobacter_subterraneus_subsp._tengcongensis_MB4 Caldanaerobacter subterraneus subsp. tengcongensis MB4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OKG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OKG FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.95&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=3okg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3okg OCA], [https://pdbe.org/3okg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3okg RCSB], [https://www.ebi.ac.uk/pdbsum/3okg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3okg 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=3okg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3okg OCA], [https://pdbe.org/3okg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3okg RCSB], [https://www.ebi.ac.uk/pdbsum/3okg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3okg ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/Q8R9Q6_CALS4 Q8R9Q6_CALS4]
Type I DNA methyltransferases contain one specificity subunit (HsdS) and two modification subunits (HsdM). The electron microscopy model of M.EcoKI-MS methyltransferase shows a reasonable closed state of this clamp-like enzyme, but the structure of the open state is still unclear. The 1.95 A crystal structure of the specificity subunit from Thermoanaerobacter tengcongensis (TTE-HsdS) shows an unreported open form inter-domain orientation of this subunit. Based on the crystal structure of TTE-HsdS and the closed state model of M.EcoKI-MS, we constructed a potential open state model of type I methyltransferase. Mutational studies indicated that two alpha-helices (aa30-59 and aa466-495) of the TTE-HsdM subunit are important inter-subunit interaction sites in the TTE-MS complex. DNA binding assays also highlighted the importance of the C-terminal region of TTE-HsdM for DNA binding by the TTE-MS complex. On the basis of structural analysis, biochemical experiments and previous studies, we propose a dynamic opening and closing mechanism for type I methyltransferase.
 
Structure of HsdS subunit from Thermoanaerobacter tengcongensis sheds lights on mechanism of dynamic opening and closing of type I methyltransferase.,Gao P, Tang Q, An X, Yan X, Liang D PLoS One. 2011 Mar 2;6(3):e17346. PMID:21399684<ref>PMID:21399684</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3okg" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Cals4]]
[[Category: Caldanaerobacter subterraneus subsp. tengcongensis MB4]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: An, X]]
[[Category: An X]]
[[Category: Gao, P]]
[[Category: Gao P]]
[[Category: Liang, D]]
[[Category: Liang D]]
[[Category: Tang, Q]]
[[Category: Tang Q]]
[[Category: Yan, X]]
[[Category: Yan X]]
[[Category: Coiled-coil]]
[[Category: Dna binding]]
[[Category: Dna binding protein]]
[[Category: Type i methyltransferase]]

Latest revision as of 11:17, 21 February 2024

Crystal structure of HsdS subunit from Thermoanaerobacter tengcongensis

3okg, resolution 1.95Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=3okg&oldid=4068425"