1mgp: Difference between revisions

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[[Image:1mgp.png|left|200px]]


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==Hypothetical protein TM841 from Thermotoga maritima reveals fatty acid binding function==
The line below this paragraph, containing "STRUCTURE_1mgp", creates the "Structure Box" on the page.
<StructureSection load='1mgp' size='340' side='right'caption='[[1mgp]], [[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'>[[1mgp]] is a 1 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=1MGP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MGP 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>
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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=PLM:PALMITIC+ACID'>PLM</scene></td></tr>
{{STRUCTURE_1mgp|  PDB=1mgp  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1mgp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mgp OCA], [https://pdbe.org/1mgp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mgp RCSB], [https://www.ebi.ac.uk/pdbsum/1mgp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mgp ProSAT], [https://www.topsan.org/Proteins/BSGC/1mgp TOPSAN]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Y1468_THEMA Y1468_THEMA] Binds long-chain fatty acids, such as palmitate, and may play a role in lipid transport or fatty acid metabolism.
== 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/mg/1mgp_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=1mgp ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
We determined the three-dimensional (3D) crystal structure of protein TM841, a protein product from a hypothetical open-reading frame in the genome of the hyperthermophile bacterium Thermotoga maritima, to 2.0 A resolution. The protein belongs to a large protein family, DegV or COG1307 of unknown function. The 35 kDa protein consists of two separate domains, with low-level structural resemblance to domains from other proteins with known 3D structures. These structural homologies, however, provided no clues for the function of TM841. But the electron density maps revealed clear density for a bound fatty-acid molecule in a pocket between the two protein domains. The structure indicates that TM841 has the molecular function of fatty-acid binding and may play a role in the cellular functions of fatty acid transport or metabolism.


===Hypothetical protein TM841 from Thermotoga maritima reveals fatty acid binding function===
Crystal structure of a hypothetical protein, TM841 of Thermotoga maritima, reveals its function as a fatty acid-binding protein.,Schulze-Gahmen U, Pelaschier J, Yokota H, Kim R, Kim SH Proteins. 2003 Mar 1;50(4):526-30. PMID:12577257<ref>PMID:12577257</ref>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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The line below this paragraph, {{ABSTRACT_PUBMED_12577257}}, adds the Publication Abstract to the page
<div class="pdbe-citations 1mgp" style="background-color:#fffaf0;"></div>
(as it appears on PubMed at http://www.pubmed.gov), where 12577257 is the PubMed ID number.
== References ==
-->
<references/>
{{ABSTRACT_PUBMED_12577257}}
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Large Structures]]
1MGP is a 1 chain 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=1MGP OCA].
 
==Reference==
Crystal structure of a hypothetical protein, TM841 of Thermotoga maritima, reveals its function as a fatty acid-binding protein., Schulze-Gahmen U, Pelaschier J, Yokota H, Kim R, Kim SH, Proteins. 2003 Mar 1;50(4):526-30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12577257 12577257]
[[Category: Thermotoga maritima]]
[[Category: Thermotoga maritima]]
[[Category: BSGC, Berkeley Structural Genomics Center.]]
[[Category: Kim R]]
[[Category: Kim, R.]]
[[Category: Kim S-H]]
[[Category: Kim, S H.]]
[[Category: Pelaschier J]]
[[Category: Pelaschier, J.]]
[[Category: Schulze-Gahmen U]]
[[Category: Schulze-Gahmen, U.]]
[[Category: Yokota H]]
[[Category: Yokota, H.]]
[[Category: Berkeley structural genomics center]]
[[Category: Bsgc structure funded by nih]]
[[Category: Protein structure initiative]]
[[Category: Psi]]
[[Category: Structural genomic]]
[[Category: Two domain structure with mixed alpha/beta structures in both domain]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Nov 16 17:37:14 2008''

Latest revision as of 07:43, 17 October 2024

Hypothetical protein TM841 from Thermotoga maritima reveals fatty acid binding functionHypothetical protein TM841 from Thermotoga maritima reveals fatty acid binding function

Structural highlights

1mgp is a 1 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

Y1468_THEMA Binds long-chain fatty acids, such as palmitate, and may play a role in lipid transport or fatty acid metabolism.

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

We determined the three-dimensional (3D) crystal structure of protein TM841, a protein product from a hypothetical open-reading frame in the genome of the hyperthermophile bacterium Thermotoga maritima, to 2.0 A resolution. The protein belongs to a large protein family, DegV or COG1307 of unknown function. The 35 kDa protein consists of two separate domains, with low-level structural resemblance to domains from other proteins with known 3D structures. These structural homologies, however, provided no clues for the function of TM841. But the electron density maps revealed clear density for a bound fatty-acid molecule in a pocket between the two protein domains. The structure indicates that TM841 has the molecular function of fatty-acid binding and may play a role in the cellular functions of fatty acid transport or metabolism.

Crystal structure of a hypothetical protein, TM841 of Thermotoga maritima, reveals its function as a fatty acid-binding protein.,Schulze-Gahmen U, Pelaschier J, Yokota H, Kim R, Kim SH Proteins. 2003 Mar 1;50(4):526-30. PMID:12577257[1]

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

References

  1. ↑ Schulze-Gahmen U, Pelaschier J, Yokota H, Kim R, Kim SH. Crystal structure of a hypothetical protein, TM841 of Thermotoga maritima, reveals its function as a fatty acid-binding protein. Proteins. 2003 Mar 1;50(4):526-30. PMID:12577257 doi:10.1002/prot.10305

1mgp, resolution 2.00Å

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