1hwu: Difference between revisions
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<StructureSection load='1hwu' size='340' side='right' caption='[[1hwu]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='1hwu' size='340' side='right' caption='[[1hwu]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1hwu]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1hwu]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_35892 Atcc 35892]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HWU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HWU FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2pii|2pii]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2pii|2pii]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GLNB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=964 | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GLNB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=964 ATCC 35892])</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=1hwu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hwu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1hwu RCSB], [http://www.ebi.ac.uk/pdbsum/1hwu PDBsum]</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=1hwu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hwu OCA], [http://pdbe.org/1hwu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1hwu RCSB], [http://www.ebi.ac.uk/pdbsum/1hwu PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 1hwu" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Atcc 35892]] | ||
[[Category: Benelli, E M]] | [[Category: Benelli, E M]] | ||
[[Category: Buck, M]] | [[Category: Buck, M]] | ||
Revision as of 06:22, 10 September 2015
STRUCTURE OF PII PROTEIN FROM HERBASPIRILLUM SEROPEDICAESTRUCTURE OF PII PROTEIN FROM HERBASPIRILLUM SEROPEDICAE
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedPII-like proteins are signal transduction proteins found in bacteria, archaea and eukaryotes. They mediate a variety of cellular responses. A second PII-like protein, called GlnK, has been found in several organisms. In the diazotroph Herbaspirillum seropedicae, PII protein is involved in sensing nitrogen levels and controlling nitrogen fixation genes. In this work, the crystal structure of the unliganded H. seropedicae PII was solved by X-ray diffraction. H. seropedicae PII has a Gly residue, Gly108 preceding Pro109 and the main-chain forms a beta turn. The glycine at position 108 allows a bend in the C-terminal main-chain, thereby modifying the surface of the cleft between monomers and potentially changing function. The structure suggests that the C-terminal region of PII proteins may be involved in specificity of function, and nonenteric diazotrophs are found to have the C-terminal consensus XGXDAX(107-112). We are also proposing binding sites for ATP and 2-oxoglutarate based on the structural alignment of PII with PII-ATP/GlnK-ATP, 5-carboxymethyl-2-hydroxymuconate isomerase and 4-oxalocrotonate tautomerase bound to the inhibitor 2-oxo-3-pentynoate. Herbaspirillum seropedicae signal transduction protein PII is structurally similar to the enteric GlnK.,Machado Benelli E, Buck M, Polikarpov I, Maltempi de Souza E, Cruz LM, Pedrosa FO Eur J Biochem. 2002 Jul;269(13):3296-303. PMID:12084071[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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