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New page: left|200px<br /><applet load="1htp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1htp, resolution 2.2Å" /> '''REFINED STRUCTURES AT...
 
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[[Image:1htp.gif|left|200px]]<br /><applet load="1htp" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1htp, resolution 2.2&Aring;" />
'''REFINED STRUCTURES AT 2 ANGSTROMS AND 2.2 ANGSTROMS OF THE TWO FORMS OF THE H-PROTEIN, A LIPOAMIDE-CONTAINING PROTEIN OF THE GLYCINE DECARBOXYLASE COMPLEX'''<br />


==Overview==
==REFINED STRUCTURES AT 2 ANGSTROMS AND 2.2 ANGSTROMS OF THE TWO FORMS OF THE H-PROTEIN, A LIPOAMIDE-CONTAINING PROTEIN OF THE GLYCINE DECARBOXYLASE COMPLEX==
Glycine decarboxylase consists of four protein components. Its structural, and mechanistic heart is provided by the lipoic acid-containing H-protein, which undergoes a cycle of reductive methylamination, methylamine transfer, and electron transfer. Lipoic acid attached to a specific lysine side, chain is assumed to act as a 'swinging arm' conveying the reactive, dithiolane ring from one catalytic centre to another. The X-ray crystal, structures of two forms of the H-protein have been determined. The lipoate, cofactor is located in the loop of a hairpin configuration but following, methylamine transfer it is pivoted to bind into a cleft at the surface of, the H-protein. The lipoamide-methylamine arm is, therefore, not free to, move in aqueous solvent.
<StructureSection load='1htp' size='340' side='right'caption='[[1htp]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1htp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HTP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HTP 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]] 2.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=OSS:6-(HYDROXYETHYLDITHIO)-8-(AMINOMETHYLTHIO)OCTANOIC+ACID'>OSS</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=1htp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1htp OCA], [https://pdbe.org/1htp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1htp RCSB], [https://www.ebi.ac.uk/pdbsum/1htp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1htp ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GCSH_PEA GCSH_PEA] The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein.
== 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/ht/1htp_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=1htp ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Glycine decarboxylase consists of four protein components. Its structural and mechanistic heart is provided by the lipoic acid-containing H-protein which undergoes a cycle of reductive methylamination, methylamine transfer and electron transfer. Lipoic acid attached to a specific lysine side chain is assumed to act as a 'swinging arm' conveying the reactive dithiolane ring from one catalytic centre to another. The X-ray crystal structures of two forms of the H-protein have been determined. The lipoate cofactor is located in the loop of a hairpin configuration but following methylamine transfer it is pivoted to bind into a cleft at the surface of the H-protein. The lipoamide-methylamine arm is, therefore, not free to move in aqueous solvent.


==About this Structure==
The lipoamide arm in the glycine decarboxylase complex is not freely swinging.,Cohen-Addad C, Pares S, Sieker L, Neuburger M, Douce R Nat Struct Biol. 1995 Jan;2(1):63-8. PMID:7719855<ref>PMID:7719855</ref>
1HTP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum] with OSS as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Glycine_dehydrogenase_(decarboxylating) Glycine dehydrogenase (decarboxylating)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.4.2 1.4.4.2] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HTP OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
The lipoamide arm in the glycine decarboxylase complex is not freely swinging., Cohen-Addad C, Pares S, Sieker L, Neuburger M, Douce R, Nat Struct Biol. 1995 Jan;2(1):63-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7719855 7719855]
</div>
[[Category: Glycine dehydrogenase (decarboxylating)]]
<div class="pdbe-citations 1htp" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pisum sativum]]
[[Category: Pisum sativum]]
[[Category: Single protein]]
[[Category: Cohen-Addad C]]
[[Category: Cohen-Addad, C.]]
[[Category: Pares S]]
[[Category: Pares, S.]]
[[Category: OSS]]
[[Category: oxidoreductases(acting on ch-nh2 donor)]]
 
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Retrieved from "https://proteopedia.org/1htp"