1woo: Difference between revisions

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New page: left|200px<br /><applet load="1woo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1woo, resolution 2.40Å" /> '''Crystal structure of...
 
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[[Image:1woo.gif|left|200px]]<br /><applet load="1woo" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1woo, resolution 2.40&Aring;" />
'''Crystal structure of T-protein of the Glycine Cleavage System'''<br />


==Overview==
==Crystal structure of T-protein of the Glycine Cleavage System==
The glycine cleavage system catalyzes the oxidative decarboxylation of, glycine in bacteria and in mitochondria of animals and plants. Its, deficiency in human causes nonketotic hyperglycinemia, an inborn error of, glycine metabolism. T-protein, one of the four components of the glycine, cleavage system,is a tetrahydrofolate dependent aminomethyltransferase. It, catalyzes the transfer of the methylene carbon unit to tetrahydrofolate, from the methylamine group covalently attached to the lipoamide arm of, H-protein. To gain insight into the T-protein function at the molecular, level, we have determined the first crystal structure of T-protein from, Thermotoga maritima by the multiwavelength anomalous diffraction method of, x-ray crystallography and refined four structures: the apoform; the, tetrahydrofolate complex; the folinic acid complex; and the lipoic acid, complex. The overall fold of T-protein is similar to that of the, C-terminal tetrahydrofolate-binding region (residues 421-830) of, Arthrobacter globiformis dimethylglycine oxidase. Tetrahydrofolate (or, folinic acid) is bound near the center of the tripartite T-protein. Lipoic, acid is bound adjacent to the tetrahydrofolate binding pocket, thus, defining the interaction surface for H-protein binding. A homology model, of the human T-protein provides the structural framework for understanding, the molecular mechanisms underlying the development of nonketotic, hyperglycinemia due to missense mutations of the human T-protein.
<StructureSection load='1woo' size='340' side='right'caption='[[1woo]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1woo]] 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=1WOO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WOO 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]] 2.4&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=THG:(6S)-5,6,7,8-TETRAHYDROFOLATE'>THG</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=1woo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1woo OCA], [https://pdbe.org/1woo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1woo RCSB], [https://www.ebi.ac.uk/pdbsum/1woo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1woo ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GCST_THEMA GCST_THEMA] The glycine cleavage system catalyzes the degradation of glycine (By similarity).
== 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/wo/1woo_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=1woo ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1WOO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with THL as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Aminomethyltransferase Aminomethyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.2.10 2.1.2.10] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1WOO OCA].
*[[Aminomethyltransferase 3D structures|Aminomethyltransferase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Crystal structure of T-protein of the glycine cleavage system. Cofactor binding, insights into H-protein recognition, and molecular basis for understanding nonketotic hyperglycinemia., Lee HH, Kim DJ, Ahn HJ, Ha JY, Suh SW, J Biol Chem. 2004 Nov 26;279(48):50514-23. Epub 2004 Sep 7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15355973 15355973]
[[Category: Large Structures]]
[[Category: Aminomethyltransferase]]
[[Category: Single protein]]
[[Category: Thermotoga maritima]]
[[Category: Thermotoga maritima]]
[[Category: Ahn, H.J.]]
[[Category: Ahn HJ]]
[[Category: Ha, J.Y.]]
[[Category: Ha JY]]
[[Category: Kim, D.J.]]
[[Category: Kim DJ]]
[[Category: Lee, H.H.]]
[[Category: Lee HH]]
[[Category: Suh, S.W.]]
[[Category: Suh SW]]
[[Category: THL]]
[[Category: glycine cleavage system]]
[[Category: t-protein]]
[[Category: tetrahydrofolate]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 05:33:58 2007''

Latest revision as of 16:33, 13 March 2024

Crystal structure of T-protein of the Glycine Cleavage SystemCrystal structure of T-protein of the Glycine Cleavage System

Structural highlights

1woo 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 2.4Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GCST_THEMA The glycine cleavage system catalyzes the degradation of glycine (By similarity).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1woo, resolution 2.40Å

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