From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:2bbk.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:2bbk.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_2bbk| PDB=2bbk | SCENE= }} | | {{STRUCTURE_2bbk| PDB=2bbk | SCENE= }} |
| | | | |
| - | '''CRYSTAL STRUCTURE OF THE QUINOPROTEIN METHYLAMINE DEHYDROGENASE FROM PARACOCCUS DENITRIFICANS AT 1.75 ANGSTROMS'''
| + | ===CRYSTAL STRUCTURE OF THE QUINOPROTEIN METHYLAMINE DEHYDROGENASE FROM PARACOCCUS DENITRIFICANS AT 1.75 ANGSTROMS=== |
| | | | |
| | | | |
| - | ==Overview==
| + | <!-- |
| - | The three-dimensional structure of the quinoprotein methylamine dehydrogenase from Paracoccus denitrificans has been refined at 1.75 A resolution utilizing the DNA-based protein sequence. The final model incorporates 8034 atoms per molecule, including 552 molecules of solvent, and gives an R-factor of 0.163. The molecule is an H2L2 hetero-tetramer containing a non-crystallographic 2-fold axis of symmetry. The 373-residue H subunit is folded into seven repeats of a four-stranded antiparallel beta-sheet motif, arranged in a propeller-like pattern about a pseudo-7-fold rotational axis of symmetry. Each L subunit contains 131 residues folded in a tight structure composed of five beta-strands in two sheets and crosslinked by six disulfide bonds. In addition there is an intrasubunit covalent linkage between two tryptophan side-chains that form the unique redox center, tryptophan tryptophylquinone (TTQ). The active site contains the O-6 carbonyl of TTQ, the side-chains of Asp32L Asp76L, Tyr119L and Thr122L, and two solvent molecules. A potential "gate" (Phe55H) separates the closed active-site cavity from a channel containing a group of highly ordered water molecules to bulk solvent. Phe55H and Tyr119L, and a number of neighboring oxygen atoms, may also provide a binding site for monovalent cations that are known to affect the reactivity and spectral properties of TTQ as well as the oxidative half reaction. The overall reaction has been dissected into a number of discrete steps that may require participation by several individual amino acid residues in the active site acting as general acids and bases.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_9514722}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 9514722 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_9514722}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 26: |
Line 30: |
| | [[Category: Mathews, F S.]] | | [[Category: Mathews, F S.]] |
| | [[Category: Electron transport]] | | [[Category: Electron transport]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 20:04:40 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 21:02:21 2008'' |
Revision as of 18:02, 28 July 2008
Template:STRUCTURE 2bbk
CRYSTAL STRUCTURE OF THE QUINOPROTEIN METHYLAMINE DEHYDROGENASE FROM PARACOCCUS DENITRIFICANS AT 1.75 ANGSTROMS
Template:ABSTRACT PUBMED 9514722
About this Structure
2BBK is a Protein complex structure of sequences from Paracoccus denitrificans. Full crystallographic information is available from OCA.
Reference
Refined crystal structure of methylamine dehydrogenase from Paracoccus denitrificans at 1.75 A resolution., Chen L, Doi M, Durley RC, Chistoserdov AY, Lidstrom ME, Davidson VL, Mathews FS, J Mol Biol. 1998 Feb 13;276(1):131-49. PMID:9514722
Page seeded by OCA on Mon Jul 28 21:02:21 2008
