1s12: Difference between revisions

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[[Image:1s12.gif|left|200px]]


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==Crystal structure of TM1457==
The line below this paragraph, containing "STRUCTURE_1s12", creates the "Structure Box" on the page.
<StructureSection load='1s12' size='340' side='right'caption='[[1s12]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1s12]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S12 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1S12 FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</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&#8491;</td></tr>
-->
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr>
{{STRUCTURE_1s12| PDB=1s12  | SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1s12 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s12 OCA], [https://pdbe.org/1s12 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1s12 RCSB], [https://www.ebi.ac.uk/pdbsum/1s12 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1s12 ProSAT], [https://www.topsan.org/Proteins/BSGC/1s12 TOPSAN]</span></td></tr>
 
</table>
'''Crystal structure of TM1457'''
== Function ==
 
[https://www.uniprot.org/uniprot/Q9X1G8_THEMA Q9X1G8_THEMA]
 
== Evolutionary Conservation ==
==Overview==
[[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/s1/1s12_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1s12 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The crystal structure of a hypothetical protein, TM1457, from Thermotoga maritima has been determined at 2.0A resolution. TM1457 belongs to the DUF464 family (57 members) for which there is no known function. The structure shows that it is composed of two helices in contact with one side of a five-stranded beta-sheet. Two identical monomers form a pseudo-dimer in the asymmetric unit. There is a large cleft between the first alpha-helix and the second beta-strand. This cleft may be functionally important, since the two highly conserved motifs, GHA and VCAXV(S/T), are located around the cleft. A structural comparison of TM1457 with known protein structures shows the best hit with another hypothetical protein, Ybl001C from Saccharomyces cerevisiae, though they share low structural similarity. Therefore, TM1457 still retains a unique topology and reveals a novel fold.
The crystal structure of a hypothetical protein, TM1457, from Thermotoga maritima has been determined at 2.0A resolution. TM1457 belongs to the DUF464 family (57 members) for which there is no known function. The structure shows that it is composed of two helices in contact with one side of a five-stranded beta-sheet. Two identical monomers form a pseudo-dimer in the asymmetric unit. There is a large cleft between the first alpha-helix and the second beta-strand. This cleft may be functionally important, since the two highly conserved motifs, GHA and VCAXV(S/T), are located around the cleft. A structural comparison of TM1457 with known protein structures shows the best hit with another hypothetical protein, Ybl001C from Saccharomyces cerevisiae, though they share low structural similarity. Therefore, TM1457 still retains a unique topology and reveals a novel fold.


==About this Structure==
Crystal structure of TM1457 from Thermotoga maritima.,Shin DH, Lou Y, Jancarik J, Yokota H, Kim R, Kim SH J Struct Biol. 2005 Nov;152(2):113-7. Epub 2005 Oct 3. PMID:16242963<ref>PMID:16242963</ref>
1S12 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S12 OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Crystal structure of TM1457 from Thermotoga maritima., Shin DH, Lou Y, Jancarik J, Yokota H, Kim R, Kim SH, J Struct Biol. 2005 Nov;152(2):113-7. Epub 2005 Oct 3. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16242963 16242963]
</div>
[[Category: Single protein]]
<div class="pdbe-citations 1s12" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thermotoga maritima]]
[[Category: Thermotoga maritima]]
[[Category: BSGC, Berkeley Structural Genomics Center.]]
[[Category: Jancarik J]]
[[Category: Jancarik, J.]]
[[Category: Kim R]]
[[Category: Kim, R.]]
[[Category: Kim S-H]]
[[Category: Kim, S H.]]
[[Category: Lou Y]]
[[Category: Lou, Y.]]
[[Category: Shin DH]]
[[Category: Shin, D H.]]
[[Category: Yokota H]]
[[Category: Yokota, H.]]
[[Category: Berkeley structural genomics center]]
[[Category: Bsgc]]
[[Category: Crystal]]
[[Category: Hypothetical protein]]
[[Category: Protein structure initiative]]
[[Category: Psi]]
[[Category: Structural genomic]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 08:09:43 2008''

Latest revision as of 10:21, 30 October 2024

Crystal structure of TM1457Crystal structure of TM1457

Structural highlights

1s12 is a 4 chain structure with sequence from Thermotoga maritima. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

Q9X1G8_THEMA

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 PubMed

The crystal structure of a hypothetical protein, TM1457, from Thermotoga maritima has been determined at 2.0A resolution. TM1457 belongs to the DUF464 family (57 members) for which there is no known function. The structure shows that it is composed of two helices in contact with one side of a five-stranded beta-sheet. Two identical monomers form a pseudo-dimer in the asymmetric unit. There is a large cleft between the first alpha-helix and the second beta-strand. This cleft may be functionally important, since the two highly conserved motifs, GHA and VCAXV(S/T), are located around the cleft. A structural comparison of TM1457 with known protein structures shows the best hit with another hypothetical protein, Ybl001C from Saccharomyces cerevisiae, though they share low structural similarity. Therefore, TM1457 still retains a unique topology and reveals a novel fold.

Crystal structure of TM1457 from Thermotoga maritima.,Shin DH, Lou Y, Jancarik J, Yokota H, Kim R, Kim SH J Struct Biol. 2005 Nov;152(2):113-7. Epub 2005 Oct 3. PMID:16242963[1]

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

References

  1. Shin DH, Lou Y, Jancarik J, Yokota H, Kim R, Kim SH. Crystal structure of TM1457 from Thermotoga maritima. J Struct Biol. 2005 Nov;152(2):113-7. Epub 2005 Oct 3. PMID:16242963 doi:10.1016/j.jsb.2005.08.008

1s12, resolution 2.00Å

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