1htp: Difference between revisions
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|PDB= 1htp |SIZE=350|CAPTION= <scene name='initialview01'>1htp</scene>, resolution 2.2Å | |PDB= 1htp |SIZE=350|CAPTION= <scene name='initialview01'>1htp</scene>, resolution 2.2Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=OSS:6-(HYDROXYETHYLDITHIO)-8-(AMINOMETHYLTHIO)OCTANOIC ACID'>OSS</scene> | |LIGAND= <scene name='pdbligand=OSS:6-(HYDROXYETHYLDITHIO)-8-(AMINOMETHYLTHIO)OCTANOIC+ACID'>OSS</scene> | ||
|ACTIVITY= [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] | |ACTIVITY= <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> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<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://www.ebi.ac.uk/pdbsum/1htp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1htp RCSB]</span> | |||
}} | }} | ||
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[[Category: Cohen-Addad, C.]] | [[Category: Cohen-Addad, C.]] | ||
[[Category: Pares, S.]] | [[Category: Pares, S.]] | ||
[[Category: oxidoreductases(acting on ch-nh2 donor)]] | [[Category: oxidoreductases(acting on ch-nh2 donor)]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:10:16 2008'' | ||
Revision as of 21:10, 30 March 2008
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| , resolution 2.2Å | |||||||
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| Ligands: | |||||||
| Activity: | Glycine dehydrogenase (decarboxylating), with EC number 1.4.4.2 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
OverviewOverview
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 StructureAbout this Structure
1HTP is a Single protein structure of sequence from Pisum sativum. Full crystallographic information is available from OCA.
ReferenceReference
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
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