1htp: Difference between revisions
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<StructureSection load='1htp' size='340' side='right'caption='[[1htp]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='1htp' size='340' side='right'caption='[[1htp]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1htp]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1htp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Garden_pea Garden pea]. 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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=OSS:6-(HYDROXYETHYLDITHIO)-8-(AMINOMETHYLTHIO)OCTANOIC+ACID'>OSS</scene></td></tr> | </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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Glycine_dehydrogenase_(decarboxylating) Glycine dehydrogenase (decarboxylating)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.4.2 1.4.4.2] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <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> | </table> | ||
== Function == | == 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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 13:53, 4 August 2021
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 COMPLEXREFINED 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
Structural highlights
Function[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 Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedGlycine 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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