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1htp

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Revision as of 10:53, 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 COMPLEX

Structural highlights

1htp is a 1 chain structure with sequence from Garden pea. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Activity:	Glycine dehydrogenase (decarboxylating), with EC number 1.4.4.2
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 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.

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

↑ Cohen-Addad C, Pares S, Sieker L, Neuburger M, Douce R. The lipoamide arm in the glycine decarboxylase complex is not freely swinging. Nat Struct Biol. 1995 Jan;2(1):63-8. PMID:7719855

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1htp"

Categories: Garden pea | Large Structures | Cohen-Addad, C | Pares, S

@@ Line 3: / Line 3: @@
 <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 [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HTP FirstGlance]. <br>
+<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'>[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] </span></td></tr>
+<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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1htp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1htp OCA], [http://pdbe.org/1htp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1htp RCSB], [http://www.ebi.ac.uk/pdbsum/1htp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1htp ProSAT]</span></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 ==
-[[http://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.
+[[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]]

1htp

From Proteopedia

Revision as of 10:53, 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 COMPLEX

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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