3nzp
From Proteopedia
(Difference between revisions)
| (6 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | [[Image:3nzp.png|left|200px]] | ||
| - | < | + | ==Crystal Structure of the Biosynthetic Arginine decarboxylase SpeA from Campylobacter jejuni, Northeast Structural Genomics Consortium Target BR53== |
| - | + | <StructureSection load='3nzp' size='340' side='right'caption='[[3nzp]], [[Resolution|resolution]] 3.00Å' scene=''> | |
| - | You may | + | == Structural highlights == |
| - | + | <table><tr><td colspan='2'>[[3nzp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Campylobacter_jejuni_subsp._jejuni_NCTC_11168_=_ATCC_700819 Campylobacter jejuni subsp. jejuni NCTC 11168 = ATCC 700819]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NZP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NZP FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3Å</td></tr> | |
| - | -- | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=3nzp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nzp OCA], [https://pdbe.org/3nzp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3nzp RCSB], [https://www.ebi.ac.uk/pdbsum/3nzp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3nzp ProSAT]</span></td></tr> | |
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q0PAC6_CAMJE Q0PAC6_CAMJE] | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nz/3nzp_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3nzp ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Biosynthetic arginine decarboxylase (ADC; also known as SpeA) plays an important role in the biosynthesis of polyamines from arginine in bacteria and plants. SpeA is a pyridoxal-5'-phosphate (PLP)-dependent enzyme and shares weak sequence homology with several other PLP-dependent decarboxylases. Here, the crystal structure of PLP-bound SpeA from Campylobacter jejuni is reported at 3.0 A resolution and that of Escherichia coli SpeA in complex with a sulfate ion is reported at 3.1 A resolution. The structure of the SpeA monomer contains two large domains, an N-terminal TIM-barrel domain followed by a beta-sandwich domain, as well as two smaller helical domains. The TIM-barrel and beta-sandwich domains share structural homology with several other PLP-dependent decarboxylases, even though the sequence conservation among these enzymes is less than 25%. A similar tetramer is observed for both C. jejuni and E. coli SpeA, composed of two dimers of tightly associated monomers. The active site of SpeA is located at the interface of this dimer and is formed by residues from the TIM-barrel domain of one monomer and a highly conserved loop in the beta-sandwich domain of the other monomer. The PLP cofactor is recognized by hydrogen-bonding, pi-stacking and van der Waals interactions. | ||
| - | + | Structures of bacterial biosynthetic arginine decarboxylases.,Forouhar F, Lew S, Seetharaman J, Xiao R, Acton TB, Montelione GT, Tong L Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Dec 1;66(Pt, 12):1562-6. Epub 2010 Nov 16. PMID:21139196<ref>PMID:21139196</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 3nzp" style="background-color:#fffaf0;"></div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | == | + | [[Category: Campylobacter jejuni subsp. jejuni NCTC 11168 = ATCC 700819]] |
| - | + | [[Category: Large Structures]] | |
| - | + | [[Category: Acton TB]] | |
| - | == | + | [[Category: Belote RL]] |
| - | < | + | [[Category: Ciccosanti C]] |
| - | [[Category: | + | [[Category: Everett JK]] |
| - | [[Category: | + | [[Category: Forouhar F]] |
| - | [[Category: Acton | + | [[Category: Hunt JF]] |
| - | [[Category: Belote | + | [[Category: Lew S]] |
| - | [[Category: Ciccosanti | + | [[Category: Montelione GT]] |
| - | [[Category: Everett | + | [[Category: Nair R]] |
| - | [[Category: Forouhar | + | [[Category: Rost B]] |
| - | [[Category: Hunt | + | [[Category: Sahdev S]] |
| - | [[Category: Lew | + | [[Category: Seetharaman J]] |
| - | [[Category: Montelione | + | [[Category: Tong L]] |
| - | + | [[Category: Xiao R]] | |
| - | [[Category: Nair | + | |
| - | [[Category: Rost | + | |
| - | [[Category: Sahdev | + | |
| - | [[Category: Seetharaman | + | |
| - | [[Category: Tong | + | |
| - | [[Category: Xiao | + | |
Current revision
Crystal Structure of the Biosynthetic Arginine decarboxylase SpeA from Campylobacter jejuni, Northeast Structural Genomics Consortium Target BR53
| |||||||||||
