1dd2

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{{Seed}}
 
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[[Image:1dd2.png|left|200px]]
 
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==BIOTIN CARBOXYL CARRIER DOMAIN OF TRANSCARBOXYLASE (TC 1.3S)==
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The line below this paragraph, containing "STRUCTURE_1dd2", creates the "Structure Box" on the page.
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<StructureSection load='1dd2' size='340' side='right'caption='[[1dd2]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1dd2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Propionibacterium_freudenreichii_subsp._shermanii Propionibacterium freudenreichii subsp. shermanii]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DD2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DD2 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dd2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dd2 OCA], [https://pdbe.org/1dd2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dd2 RCSB], [https://www.ebi.ac.uk/pdbsum/1dd2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dd2 ProSAT]</span></td></tr>
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{{STRUCTURE_1dd2| PDB=1dd2 | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/BCCP_PROFR BCCP_PROFR] The biotinyl 1.3S subunit serves as a carboxyl carrier between the substrate-binding sites on the 12S and 5S subunits.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dd/1dd2_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1dd2 ConSurf].
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<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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Transcarboxylase (TC) from Propionibacterium shermanii, a biotin-dependent enzyme, catalyzes the transfer of a carboxyl group from methylmalonyl-CoA to pyruvate to form propionyl-CoA and oxalacetate. Within the multi-subunit enzyme complex, the 1.3S subunit functions as the carboxyl group carrier and also binds the other two subunits to assist in the overall assembly of the enzyme. The 1.3S subunit is a 123 amino acid polypeptide (12.6 kDa) to which biotin is covalently attached at Lys 89. The three-dimensional solution structure of the full-length holo-1.3S subunit of TC has been solved by multidimensional heteronuclear NMR spectroscopy. The C-terminal half of the protein (51-123) is folded into a compact all-beta-domain comprising of two four-stranded antiparallel beta-sheets connected by short loops and turns. The fold exhibits a high 2-fold internal symmetry and is similar to that of the biotin carboxyl carrier protein (BCCP) of acetyl-CoA carboxylase, but lacks an extension that has been termed "protruding thumb" in BCCP. The first 50 residues, which have been shown to be involved in intersubunit interactions in the intact enzyme, appear to be disordered in the isolated 1.3S subunit. The molecular surface of the folded domain has two distinct surfaces: one side is highly charged, while the other comprises mainly hydrophobic, highly conserved residues.
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===BIOTIN CARBOXYL CARRIER DOMAIN OF TRANSCARBOXYLASE (TC 1.3S)===
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High resolution solution structure of the 1.3S subunit of transcarboxylase from Propionibacterium shermanii.,Reddy DV, Shenoy BC, Carey PR, Sonnichsen FD Biochemistry. 2000 Mar 14;39(10):2509-16. PMID:10704200<ref>PMID:10704200</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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The line below this paragraph, {{ABSTRACT_PUBMED_10704200}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1dd2" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 10704200 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_10704200}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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1DD2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Propionibacterium_freudenreichii_subsp._shermanii Propionibacterium freudenreichii subsp. shermanii]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DD2 OCA].
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==Reference==
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High resolution solution structure of the 1.3S subunit of transcarboxylase from Propionibacterium shermanii., Reddy DV, Shenoy BC, Carey PR, Sonnichsen FD, Biochemistry. 2000 Mar 14;39(10):2509-16. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10704200 10704200]
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[[Category: Methylmalonyl-CoA carboxytransferase]]
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[[Category: Propionibacterium freudenreichii subsp. shermanii]]
[[Category: Propionibacterium freudenreichii subsp. shermanii]]
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[[Category: Single protein]]
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[[Category: Carey PR]]
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[[Category: Carey, P R.]]
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[[Category: Reddy DV]]
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[[Category: Reddy, D V.]]
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[[Category: Shenoy BC]]
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[[Category: Shenoy, B C.]]
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[[Category: Sonnichsen FD]]
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[[Category: Sonnichsen, F D.]]
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[[Category: Antiparallel beta sheet]]
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[[Category: Biocytin]]
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[[Category: Hammerhead]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 22:50:46 2008''
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Current revision

BIOTIN CARBOXYL CARRIER DOMAIN OF TRANSCARBOXYLASE (TC 1.3S)

PDB ID 1dd2

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