|
|
| (8 intermediate revisions not shown.) |
| Line 1: |
Line 1: |
| - | [[Image:2afk.gif|left|200px]] | + | #REDIRECT [[4wzb]] This PDB entry is obsolete and replaced by 4wzb |
| - | | + | |
| - | {{Structure
| + | |
| - | |PDB= 2afk |SIZE=350|CAPTION= <scene name='initialview01'>2afk</scene>, resolution 2.30Å
| + | |
| - | |SITE=
| + | |
| - | |LIGAND= <scene name='pdbligand=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CFN:FE(7)-MO-S(9)-N+CLUSTER'>CFN</scene>, <scene name='pdbligand=CLF:FE(8)-S(7)+CLUSTER'>CLF</scene>, <scene name='pdbligand=HCA:3-HYDROXY-3-CARBOXY-ADIPIC+ACID'>HCA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>
| + | |
| - | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Nitrogenase Nitrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.18.6.1 1.18.6.1] </span>
| + | |
| - | |GENE=
| + | |
| - | |DOMAIN=
| + | |
| - | |RELATEDENTRY=[[2afh|2AFH]], [[2afi|2AFI]]
| + | |
| - | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2afk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2afk OCA], [http://www.ebi.ac.uk/pdbsum/2afk PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2afk RCSB]</span>
| + | |
| - | }}
| + | |
| - | | + | |
| - | '''Crystal Structure of MgAMPPCP-bound Av2-Av1 complex'''
| + | |
| - | | + | |
| - | | + | |
| - | ==Overview==
| + | |
| - | Adenosine triphosphate (ATP) hydrolysis in the nitrogenase complex controls the cycle of association and dissociation between the electron donor adenosine triphosphatase (ATPase) (Fe-protein) and its target catalytic protein (MoFe-protein), driving the reduction of dinitrogen into ammonia. Crystal structures in different nucleotide states have been determined that identify conformational changes in the nitrogenase complex during ATP turnover. These structures reveal distinct and mutually exclusive interaction sites on the MoFe-protein surface that are selectively populated, depending on the Fe-protein nucleotide state. A consequence of these different docking geometries is that the distance between redox cofactors, a critical determinant of the intermolecular electron transfer rate, is coupled to the nucleotide state. More generally, stabilization of distinct docking geometries by different nucleotide states, as seen for nitrogenase, could enable nucleotide hydrolysis to drive the relative motion of protein partners in molecular motors and other systems.
| + | |
| - | | + | |
| - | ==About this Structure==
| + | |
| - | 2AFK is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AFK OCA].
| + | |
| - | | + | |
| - | ==Reference==
| + | |
| - | Nitrogenase complexes: multiple docking sites for a nucleotide switch protein., Tezcan FA, Kaiser JT, Mustafi D, Walton MY, Howard JB, Rees DC, Science. 2005 Aug 26;309(5739):1377-80. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16123301 16123301]
| + | |
| - | [[Category: Azotobacter vinelandii]]
| + | |
| - | [[Category: Nitrogenase]]
| + | |
| - | [[Category: Protein complex]]
| + | |
| - | [[Category: Howard, J B.]]
| + | |
| - | [[Category: Kaiser, J T.]]
| + | |
| - | [[Category: Mustafi, D.]]
| + | |
| - | [[Category: Rees, D C.]]
| + | |
| - | [[Category: Tezcan, F A.]]
| + | |
| - | [[Category: Walton, M Y.]]
| + | |
| - | [[Category: iron-sulfur]]
| + | |
| - | [[Category: metal-binding]]
| + | |
| - | [[Category: molybdenum]]
| + | |
| - | [[Category: nitrogen fixation]]
| + | |
| - | [[Category: oxidoreductase]]
| + | |
| - | | + | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:51:59 2008''
| + | |
