1tu2

<StructureSection load='1tu2' size='340' side='right'caption='[[1tu2]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[1tu2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Anabaena_pcc7119 Anabaena pcc7119]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TU2 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1TU2 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PETE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1168 Anabaena PCC7119]), PETA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1168 Anabaena PCC7119])</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=1tu2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tu2 OCA], [http://pdbe.org/1tu2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1tu2 RCSB], [http://www.ebi.ac.uk/pdbsum/1tu2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1tu2 ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/PLAS_NOSS1 PLAS_NOSS1]] Participates in electron transfer between P700 and the cytochrome b6-f complex in photosystem I. [[http://www.uniprot.org/uniprot/CYF_NOSS1 CYF_NOSS1]] Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions (By similarity).

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== Publication Abstract from PubMed ==

The complex between cytochrome f and plastocyanin from the cyanobacterium Nostoc has been characterized by NMR spectroscopy. The binding constant is 16 mM(-1), and the lifetime of the complex is much less than 10 ms. Intermolecular pseudo-contact shifts observed for the plastocyanin amide nuclei, caused by the heme iron, as well as the chemical-shift perturbation data were used as the sole experimental restraints to determine the orientation of plastocyanin relative to cytochrome f with a precision of 1.3 angstroms. The data show that the hydrophobic patch surrounding tyrosine 1 in cytochrome f docks the hydrophobic patch of plastocyanin. Charge complementarities are found between the rims of the respective recognition sites of cytochrome f and plastocyanin. Significant differences in the relative orientation of both proteins are found between this complex and those previously reported for plants and Phormidium, indicating that electrostatic and hydrophobic interactions are balanced differently in these complexes.

Structure of the complex between plastocyanin and cytochrome f from the cyanobacterium Nostoc sp. PCC 7119 as determined by paramagnetic NMR. The balance between electrostatic and hydrophobic interactions within the transient complex determines the relative orientation of the two proteins.,Diaz-Moreno I, Diaz-Quintana A, De la Rosa MA, Ubbink M J Biol Chem. 2005 May 13;280(19):18908-15. Epub 2005 Feb 10. PMID:15705583<ref>PMID:15705583</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1tu2" style="background-color:#fffaf0;"></div>

[[Category: Anabaena pcc7119]]

[[Category: Diaz-Moreno, I]]

[[Category: Diaz-Quintana, A]]

[[Category: Rosa, M A.De la]]

[[Category: Ubbink, M]]

[[Category: Chemical shift]]

[[Category: Complex formation]]

[[Category: Pseudocontact shift]]