1ot6

<table><tr><td colspan='2'>[[1ot6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Dsm_244 Dsm 244]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OT6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OT6 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HC4:4-HYDROXYCINNAMIC+ACID'>HC4</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ot9|1ot9]], [[1ota|1ota]], [[1otb|1otb]], [[1ot1|1ot1]], [[1ote|1ote]], [[1otd|1otd]]</td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PYP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1053 DSM 244])</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=1ot6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ot6 OCA], [http://pdbe.org/1ot6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ot6 RCSB], [http://www.ebi.ac.uk/pdbsum/1ot6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ot6 ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/PYP_HALHA PYP_HALHA]] Photoactive blue light protein. Probably functions as a photoreceptor for a negative phototaxis response.

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== Publication Abstract from PubMed ==

Eight high-resolution crystal structures of the ground state of photoactive yellow protein (PYP) solved under a variety of conditions reveal that its chromophore is stabilized by two unusually short hydrogen bonds. Both Tyr42 Oeta and Glu46 Oepsilon are separated from the chromophore phenolate oxygen by less than the sum of their atomic van der Waals radii, 2.6 angstroms. This is characteristic of strong hydrogen bonding, in which hydrogen bonds acquire significant covalent character. The hydrogen bond from the protonated Glu46 to the negatively charged phenolate oxygen is 2.58 +/- 0.01 angstroms in length, while that from Tyr42 is considerably shorter, 2.49 +/- 0.01 angstroms. The E46Q mutant was solved to 0.95 angstroms resolution; the isosteric mutation increased the length of the hydrogen bond from Glx46 to the chromophore by 0.29 +/- 0.01 angstroms to that of an average hydrogen bond, 2.88 +/- 0.01 angstroms. The very short hydrogen bond from Tyr42 explains why mutating this residue has such a severe effect on the ground-state structure and PYP photocycle. The effect of isosteric mutations on the photocycle can be largely explained by the alterations to the length and strength of these hydrogen bonds.

Short hydrogen bonds in photoactive yellow protein.,Anderson S, Crosson S, Moffat K Acta Crystallogr D Biol Crystallogr. 2004 Jun;60(Pt 6):1008-16. Epub 2004, May 21. PMID:15159559<ref>PMID:15159559</ref>

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

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== References ==

<references/>

[[Category: Dsm 244]]

[[Category: Anderson, S]]

[[Category: Crosson, S]]

[[Category: Moffat, K]]

[[Category: Signaling protein]]