1w3d
From Proteopedia
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|SITE= | |SITE= | ||
|LIGAND= | |LIGAND= | ||
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Dihydrolipoyllysine-residue_acetyltransferase Dihydrolipoyllysine-residue acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.12 2.3.1.12] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydrolipoyllysine-residue_acetyltransferase Dihydrolipoyllysine-residue acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.12 2.3.1.12] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1w3d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w3d OCA], [http://www.ebi.ac.uk/pdbsum/1w3d PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1w3d RCSB]</span> | ||
}} | }} | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:30:35 2008'' |
Revision as of 21:30, 30 March 2008
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| Activity: | Dihydrolipoyllysine-residue acetyltransferase, with EC number 2.3.1.12 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
NMR STRUCTURE OF THE PERIPHERAL-SUBUNIT BINDING DOMAIN OF BACILLUS STEAROTHERMOPHILUS E2P
Overview
A (15)N-labelled peripheral-subunit binding domain (PSBD) of the dihydrolipoyl acetyltransferase (E2p) and the dimer of a solubilized interface domain (E3int) derived from the dihydrolipoyl dehydrogenase (E3) were used to investigate the basis of the interaction of E2p with E3 in the assembly of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus. Thirteen of the 55 amino acids in the PSBD show significant changes in either or both of the (15)N and (1)H amide chemical shifts when the PSBD forms a 1 : 1 complex with E3int. All of the 13 amino acids reside near the N-terminus of helix I of PSBD or in the loop region between helix II and helix III. (15)N backbone dynamics experiments on PSBD indicate that the structured region extends from Val129 to Ala168, with limited structure present in residues Asn126 to Arg128. The presence of structure in the region before helix I was confirmed by a refinement of the NMR structure of uncomplexed PSBD. Comparison of the crystal structure of the PSBD bound to E3 with the solution structure of uncomplexed PSBD described here indicates that the PSBD undergoes almost no conformational change upon binding to E3. These studies exemplify and validate the novel use of a solubilized, truncated protein domain in overcoming the limitations of high molecular mass on NMR spectroscopy.
About this Structure
1W3D is a Single protein structure of sequence from Geobacillus stearothermophilus. Full crystallographic information is available from OCA.
Reference
Interaction of the E2 and E3 components of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus. Use of a truncated protein domain in NMR spectroscopy., Allen MD, Broadhurst RW, Solomon RG, Perham RN, FEBS J. 2005 Jan;272(1):259-68. PMID:15634348
Page seeded by OCA on Mon Mar 31 00:30:35 2008
Categories: Dihydrolipoyllysine-residue acetyltransferase | Geobacillus stearothermophilus | Single protein | Allen, M D. | Broadhurst, R W. | Perham, R G.Solomon and R N. | Acyltransferase | Bacillus sterothermophilus | Dihydrolipoamide acetyltransferase | Dihydrolipoamide dehydrogenase | Glycolysis | Lipoyl | Multienzyme complex | Nmr | Peripheral-subunit binding domain | Protein structure | Protein-protein interaction | Transferase
