1x77

<StructureSection load='1x77' size='340' side='right'caption='[[1x77]], [[Resolution|resolution]] 2.70&Aring;' scene=''>

<table><tr><td colspan='2'>[[1x77]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseae Pseae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X77 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1X77 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</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=1x77 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x77 OCA], [http://pdbe.org/1x77 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1x77 RCSB], [http://www.ebi.ac.uk/pdbsum/1x77 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1x77 ProSAT], [http://www.topsan.org/Proteins/NYSGXRC/1x77 TOPSAN]</span></td></tr>

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

The availability of high-intensity synchrotron facilities, technological advances in data-collection techniques and improved data-reduction and crystallographic software have ushered in a new era in high-throughput macromolecular crystallography. Here, the de novo automated crystal structure determination at 1.28 A resolution of an NAD(P)H-dependent FMN reductase flavoprotein from Pseudomonas aeruginosa PA01-derived protein Q9I4D4 using the anomalous signal from an unusually small number of S atoms is reported. Although this protein lacks the flavodoxin key fingerprint motif [(T/S)XTGXT], it has been confirmed to bind flavin mononucleotide and the binding site was identified via X-ray crystallography. This protein contains a novel flavin mononucleotide-binding site GSLRSGSYN, which has not been previously reported. Detailed statistics pertaining to sulfur phasing and other factors contributing to structure determination are discussed. Structural comparisons of the apoenzyme and the protein complexed with flavin mononucleotide show conformational changes on cofactor binding. NADPH-dependent activity has been confirmed with biochemical assays.

Structure determination of an FMN reductase from Pseudomonas aeruginosa PA01 using sulfur anomalous signal.,Agarwal R, Bonanno JB, Burley SK, Swaminathan S Acta Crystallogr D Biol Crystallogr. 2006 Apr;62(Pt 4):383-91. Epub 2006, Mar 18. PMID:16552139<ref>PMID:16552139</ref>

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

</div>

<div class="pdbe-citations 1x77" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Agarwal, R]]

[[Category: Burley, S K]]

[[Category: Structural genomic]]

[[Category: Swaminathan, S]]

[[Category: Unknown function]]