3e35

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{{Seed}}
 
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[[Image:3e35.jpg|left|200px]]
 
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==Actinobacteria-specific protein of unknown function, SCO1997==
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The line below this paragraph, containing "STRUCTURE_3e35", creates the "Structure Box" on the page.
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<StructureSection load='3e35' size='340' side='right'caption='[[3e35]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3e35]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_coelicolor_A3(2) Streptomyces coelicolor A3(2)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E35 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3E35 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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{{STRUCTURE_3e35| PDB=3e35 | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3e35 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e35 OCA], [https://pdbe.org/3e35 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3e35 RCSB], [https://www.ebi.ac.uk/pdbsum/3e35 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3e35 ProSAT]</span></td></tr>
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</table>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e3/3e35_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=3e35 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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BACKGROUND: The Actinobacteria phylum represents one of the largest and most diverse groups of bacteria, encompassing many important and well-characterized organisms including Streptomyces, Bifidobacterium, Corynebacterium and Mycobacterium. Members of this phylum are remarkably diverse in terms of life cycle, morphology, physiology and ecology. Recent comparative genomic analysis of 19 actinobacterial species determined that only 5 genes of unknown function uniquely define this large phylum 1. The cellular functions of these actinobacteria-specific proteins (ASP) are not known. RESULTS: Here we report the first characterization of one of the 5 actinobacteria-specific proteins, ASP1 (Gene ID: SCO1997) from Streptomyces coelicolor. The X-ray crystal structure of ASP1 was determined at 2.2 A. The overall structure of ASP1 retains a similar fold to the large NP-1 family of nucleoside phosphorylase enzymes; however, the function is not related. Further comparative analysis revealed two regions expected to be important for protein function: a central, divalent metal ion binding pore, and a highly conserved elbow shaped helical region at the C-terminus. Sequence analyses revealed that ASP1 is paralogous to another actinobacteria-specific protein ASP2 (SCO1662 from S. coelicolor) and that both proteins likely carry out similar function. CONCLUSION: Our structural data in combination with sequence analysis supports the idea that two of the 5 actinobacteria-specific proteins, ASP1 and ASP2, mediate similar function. This function is predicted to be novel since the structures of these proteins do not match any known protein with or without known function. Our results suggest that this function could involve divalent metal ion binding/transport.
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===Actinobacteria-specific protein of unknown function, SCO1997===
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Structural and phylogenetic analysis of a conserved actinobacteria-specific protein (ASP1; SCO1997) from Streptomyces coelicolor.,Gao B, Sugiman-Marangos S, Junop MS, Gupta RS BMC Struct Biol. 2009 Jun 10;9:40. PMID:19515238<ref>PMID:19515238</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==About this Structure==
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</div>
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3E35 is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Bacteria Bacteria]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E35 OCA].
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<div class="pdbe-citations 3e35" style="background-color:#fffaf0;"></div>
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[[Category: Bacteria]]
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== References ==
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[[Category: Gao, B.]]
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<references/>
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[[Category: Gupta, R S.]]
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__TOC__
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[[Category: Junop, M S.]]
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</StructureSection>
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[[Category: Sugiman-Marangos, S N.]]
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[[Category: Large Structures]]
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[[Category: Actinobacteria-specific protein]]
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[[Category: Gao B]]
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[[Category: Alpha/beta/alpha structure]]
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[[Category: Gupta RS]]
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[[Category: Conserved protein]]
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[[Category: Junop MS]]
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[[Category: Unknown function]]
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[[Category: Sugiman-Marangos S]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jun 25 11:18:09 2009''
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Current revision

Actinobacteria-specific protein of unknown function, SCO1997

PDB ID 3e35

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