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| | <StructureSection load='1ojt' size='340' side='right'caption='[[1ojt]], [[Resolution|resolution]] 2.75Å' scene=''> | | <StructureSection load='1ojt' size='340' side='right'caption='[[1ojt]], [[Resolution|resolution]] 2.75Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1ojt]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"diplokokkus_intracellularis_meningitidis"_(sic)_weichselbaum_1887 "diplokokkus intracellularis meningitidis" (sic) weichselbaum 1887]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OJT OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1OJT FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1ojt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Neisseria_meningitidis Neisseria meningitidis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OJT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OJT FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.75Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">M-6 OBTAINED FROM A GENOMIC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=487 "Diplokokkus intracellularis meningitidis" (sic) Weichselbaum 1887])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1ojt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ojt OCA], [http://pdbe.org/1ojt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ojt RCSB], [http://www.ebi.ac.uk/pdbsum/1ojt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ojt 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=1ojt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ojt OCA], [https://pdbe.org/1ojt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ojt RCSB], [https://www.ebi.ac.uk/pdbsum/1ojt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ojt ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q51225_NEIME Q51225_NEIME] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Pernot, L]] | + | [[Category: Neisseria meningitidis]] |
| - | [[Category: Prange, T]] | + | [[Category: Li De La Sierra I]] |
| - | [[Category: Sierra, I Li De La]]
| + | [[Category: Pernot L]] |
| - | [[Category: Fad]] | + | [[Category: Prange T]] |
| - | [[Category: Flavoprotein]] | + | |
| - | [[Category: Glycolysis]]
| + | |
| - | [[Category: Nad]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: P64k]]
| + | |
| - | [[Category: Redox-active center]]
| + | |
| Structural highlights
Function
Q51225_NEIME
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
The protein p64k from the surface of the Neisseria meningitidis bacteria has been characterized as a two-domain protein. It contains a dihydrolipoamide dehydrogenase domain of 482 residues, involving a FAD prosthetic group as a cofactor, and a smaller lipoic acid binding domain of 86 residues. The two domains are joined by a flexible segment rich in alanine and proline residues. The structure of the dihydrolipoamide dehydrogenase domain was determined by X-ray diffraction. It was solved by a combination of molecular replacement and multiple isomorphous replacement techniques and refined to 2.7 A resolution. In the crystal, the recombinant p64k mimics the functional homo-dimer by using one of the crystallographic 2-fold axes. The reactive disulphide bridge Cys161-Cys166 is in the oxidised state and the FAD is bound in an extended conformation. This main domain contains the major antigenic determinant of the protein, an extended loop of 32 residues at the surface of the protein. A mis-attribution at residue 553 in the sequence has been detected by inspection of electron density maps and the geometry. However, when compared to the other dihydrolipoamide dehydrogenases, there are some significant differences: (1) an unusual number of cis-proline residues and (2) a new motif built around a 2-fold axis by the sulphur atoms of residues Met558, Cys560 and their symmetry related equivalents.
Molecular structure of the lipoamide dehydrogenase domain of a surface antigen from Neisseria meningitidis.,Li de la Sierra I, Pernot L, Prange T, Saludjian P, Schiltz M, Fourme R, Padron G J Mol Biol. 1997 May 30;269(1):129-41. PMID:9193005[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Li de la Sierra I, Pernot L, Prange T, Saludjian P, Schiltz M, Fourme R, Padron G. Molecular structure of the lipoamide dehydrogenase domain of a surface antigen from Neisseria meningitidis. J Mol Biol. 1997 May 30;269(1):129-41. PMID:9193005
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