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| | ==CRYSTAL STRUCTURE OF A FDXN ELEMENT EXCISION CONTROLLING FACTOR PROTEIN (AVA_3312) FROM ANABAENA VARIABILIS AT 1.60 A RESOLUTION== | | ==CRYSTAL STRUCTURE OF A FDXN ELEMENT EXCISION CONTROLLING FACTOR PROTEIN (AVA_3312) FROM ANABAENA VARIABILIS AT 1.60 A RESOLUTION== |
| - | <StructureSection load='2okf' size='340' side='right' caption='[[2okf]], [[Resolution|resolution]] 1.60Å' scene=''> | + | <StructureSection load='2okf' size='340' side='right'caption='[[2okf]], [[Resolution|resolution]] 1.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2okf]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Anava Anava]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OKF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2OKF FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2okf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Trichormus_variabilis Trichormus variabilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OKF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OKF FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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]] 1.6Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">YP_323815.1, Ava_3312 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1172 ANAVA])</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=2okf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2okf OCA], [https://pdbe.org/2okf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2okf RCSB], [https://www.ebi.ac.uk/pdbsum/2okf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2okf ProSAT], [https://www.topsan.org/Proteins/JCSG/2okf TOPSAN]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2okf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2okf OCA], [http://pdbe.org/2okf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2okf RCSB], [http://www.ebi.ac.uk/pdbsum/2okf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2okf ProSAT], [http://www.topsan.org/Proteins/JCSG/2okf TOPSAN]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q3M7W6_TRIV2 Q3M7W6_TRIV2] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Anava]] | + | [[Category: Large Structures]] |
| - | [[Category: Structural genomic]] | + | [[Category: Trichormus variabilis]] |
| - | [[Category: Dna binding protein]]
| + | |
| - | [[Category: Fdxn element excision controlling factor protein]]
| + | |
| - | [[Category: Jcsg]]
| + | |
| - | [[Category: PSI, Protein structure initiative]]
| + | |
| - | [[Category: Xish protein]]
| + | |
| Structural highlights
2okf is a 2 chain structure with sequence from Trichormus variabilis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 1.6Å |
| Ligands: | , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN |
Function
Q3M7W6_TRIV2
Publication Abstract from PubMed
Nitrogen fixation is an important process that converts atmospheric gaseous nitrogen, a form plants cannot utilize, into ammonia that can be easily assimilated. Large serine recombinase XisF (fdxN element site-specific recombinase), together with controlling factors XisH and XisI, plays a critical role in the expression of nitrogen fixation genes of certain Anabaena and Nostoc species of cyanobacteria. All three proteins are required to excise the fdxN DNA element from the chromosome in differentiating heterocysts for the expression of nitrogen fixation related genes. We report the first crystal structures of XisH and XisI proteins, both adopting novel protein folds. Based on the analysis of their sequences and structures, we propose that XisH and XisI proteins function as endonucleases and recombination directionality factors (RDFs), respectively. (c) Proteins 2014;. (c) 2014 Wiley Periodicals, Inc.
Site-specific recombination of nitrogen-fixation genes in cyanobacteria by XisF-XisH-XisI complex: Structures and models.,Hwang WC, Golden JW, Pascual J, Xu D, Cheltsov A, Godzik A Proteins. 2014 Sep 1. doi: 10.1002/prot.24679. PMID:25179344[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hwang WC, Golden JW, Pascual J, Xu D, Cheltsov A, Godzik A. Site-specific recombination of nitrogen-fixation genes in cyanobacteria by XisF-XisH-XisI complex: Structures and models. Proteins. 2014 Sep 1. doi: 10.1002/prot.24679. PMID:25179344 doi:http://dx.doi.org/10.1002/prot.24679
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