3cm1

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of SsgA-like sporulation-specific cell division protein (YP_290167.1) from Thermobifida fusca YX-ER1 at 2.60 A resolution

Structural highlights

3cm1 is a 3 chain structure with sequence from Thermobifida fusca YX. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.6Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

SSGB_THEFY Involved in sporulation-specific cell division (PubMed:19567872). Required for early stages of sporulation. Important in the process of growth cessation prior to sporulation-specific cell division. Recruits cell division protein FtsZ to the future septum sites and tethers the contractile ring structure (Z ring) to the cytoplasmic membrane during sporulation (By similarity). Stimulates polymerization and filament length of FtsZ in vitro (PubMed:21205868).[UniProtKB:Q9L268]^[1] ^[2]

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 PubMed

SsgA-like proteins (SALPs) are a family of homologous cell division-related proteins that occur exclusively in morphologically complex actinomycetes. We show that SsgB, a subfamily of SALPs, is the archetypal SALP that is functionally conserved in all sporulating actinomycetes. Sporulation-specific cell division of Streptomyces coelicolor ssgB mutants is restored by introduction of distant ssgB orthologues from other actinomycetes. Interestingly, the number of septa (and spores) of the complemented null mutants is dictated by the specific ssgB orthologue that is expressed. The crystal structure of the SsgB from Thermobifida fusca was determined at 2.6 A resolution and represents the first structure for this family. The structure revealed similarities to a class of eukaryotic "whirly" single-stranded DNA/RNA-binding proteins. However, the electro-negative surface of the SALPs suggests that neither SsgB nor any of the other SALPs are likely to interact with nucleotide substrates. Instead, we show that a conserved hydrophobic surface is likely to be important for SALP function and suggest that proteins are the likely binding partners.

Structural and functional characterizations of SsgB, a conserved activator of developmental cell division in morphologically complex actinomycetes.,Xu Q, Traag BA, Willemse J, McMullan D, Miller MD, Elsliger MA, Abdubek P, Astakhova T, Axelrod HL, Bakolitsa C, Carlton D, Chen C, Chiu HJ, Chruszcz M, Clayton T, Das D, Deller MC, Duan L, Ellrott K, Ernst D, Farr CL, Feuerhelm J, Grant JC, Grzechnik A, Grzechnik SK, Han GW, Jaroszewski L, Jin KK, Klock HE, Knuth MW, Kozbial P, Krishna SS, Kumar A, Marciano D, Minor W, Mommaas AM, Morse AT, Nigoghossian E, Nopakun A, Okach L, Oommachen S, Paulsen J, Puckett C, Reyes R, Rife CL, Sefcovic N, Tien HJ, Trame CB, van den Bedem H, Wang S, Weekes D, Hodgson KO, Wooley J, Deacon AM, Godzik A, Lesley SA, Wilson IA, van Wezel GP J Biol Chem. 2009 Sep 11;284(37):25268-79. Epub 2009 Jun 30. PMID:19567872^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Xu Q, Traag BA, Willemse J, McMullan D, Miller MD, Elsliger MA, Abdubek P, Astakhova T, Axelrod HL, Bakolitsa C, Carlton D, Chen C, Chiu HJ, Chruszcz M, Clayton T, Das D, Deller MC, Duan L, Ellrott K, Ernst D, Farr CL, Feuerhelm J, Grant JC, Grzechnik A, Grzechnik SK, Han GW, Jaroszewski L, Jin KK, Klock HE, Knuth MW, Kozbial P, Krishna SS, Kumar A, Marciano D, Minor W, Mommaas AM, Morse AT, Nigoghossian E, Nopakun A, Okach L, Oommachen S, Paulsen J, Puckett C, Reyes R, Rife CL, Sefcovic N, Tien HJ, Trame CB, van den Bedem H, Wang S, Weekes D, Hodgson KO, Wooley J, Deacon AM, Godzik A, Lesley SA, Wilson IA, van Wezel GP. Structural and functional characterizations of SsgB, a conserved activator of developmental cell division in morphologically complex actinomycetes. J Biol Chem. 2009 Sep 11;284(37):25268-79. Epub 2009 Jun 30. PMID:19567872 doi:10.1074/jbc.M109.018564
↑ Willemse J, Borst JW, de Waal E, Bisseling T, van Wezel GP. Positive control of cell division: FtsZ is recruited by SsgB during sporulation of Streptomyces. Genes Dev. 2011 Jan 1;25(1):89-99. doi: 10.1101/gad.600211. PMID:21205868 doi:http://dx.doi.org/10.1101/gad.600211
↑ Xu Q, Traag BA, Willemse J, McMullan D, Miller MD, Elsliger MA, Abdubek P, Astakhova T, Axelrod HL, Bakolitsa C, Carlton D, Chen C, Chiu HJ, Chruszcz M, Clayton T, Das D, Deller MC, Duan L, Ellrott K, Ernst D, Farr CL, Feuerhelm J, Grant JC, Grzechnik A, Grzechnik SK, Han GW, Jaroszewski L, Jin KK, Klock HE, Knuth MW, Kozbial P, Krishna SS, Kumar A, Marciano D, Minor W, Mommaas AM, Morse AT, Nigoghossian E, Nopakun A, Okach L, Oommachen S, Paulsen J, Puckett C, Reyes R, Rife CL, Sefcovic N, Tien HJ, Trame CB, van den Bedem H, Wang S, Weekes D, Hodgson KO, Wooley J, Deacon AM, Godzik A, Lesley SA, Wilson IA, van Wezel GP. Structural and functional characterizations of SsgB, a conserved activator of developmental cell division in morphologically complex actinomycetes. J Biol Chem. 2009 Sep 11;284(37):25268-79. Epub 2009 Jun 30. PMID:19567872 doi:10.1074/jbc.M109.018564

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3cm1"

Categories: Large Structures | Thermobifida fusca YX | Chruszcz M | Minor W | Wang S

@@ Line 3: / Line 3: @@
 <StructureSection load='3cm1' size='340' side='right'caption='[[3cm1]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3cm1]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Thefy Thefy]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CM1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CM1 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3cm1]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermobifida_fusca_YX Thermobifida fusca YX]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CM1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CM1 FirstGlance]. <br>
-</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">YP_290167.1, Tfu_2111 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=269800 THEFY])</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></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=3cm1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cm1 OCA], [https://pdbe.org/3cm1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3cm1 RCSB], [https://www.ebi.ac.uk/pdbsum/3cm1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3cm1 ProSAT], [https://www.topsan.org/Proteins/JCSG/3cm1 TOPSAN]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/SSGB_THEFY SSGB_THEFY] Involved in sporulation-specific cell division (PubMed:19567872). Required for early stages of sporulation. Important in the process of growth cessation prior to sporulation-specific cell division. Recruits cell division protein FtsZ to the future septum sites and tethers the contractile ring structure (Z ring) to the cytoplasmic membrane during sporulation (By similarity). Stimulates polymerization and filament length of FtsZ in vitro (PubMed:21205868).[UniProtKB:Q9L268]<ref>PMID:19567872</ref> <ref>PMID:21205868</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 13: / Line 15: @@
   <jmolCheckbox>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cm/3cm1_consurf.spt"</scriptWhenChecked>
-    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
@@ Line 32: / Line 34: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Thefy]]
+[[Category: Thermobifida fusca YX]]
-[[Category: Chruszcz, M]]
+[[Category: Chruszcz M]]
-[[Category: Structural genomic]]
+[[Category: Minor W]]
-[[Category: Minor, W]]
+[[Category: Wang S]]
-[[Category: Wang, S]]
-[[Category: Cell cycle]]
-[[Category: Jcsg]]
-[[Category: PSI, Protein structure initiative]]
-[[Category: Ssga]]
-[[Category: Ssga-like sporulation-specific cell division protein]]
-[[Category: Streptomyces sporulation and cell division protein]]
-[[Category: Yp_290167 1]]

3cm1

From Proteopedia

Current revision

Crystal structure of SsgA-like sporulation-specific cell division protein (YP_290167.1) from Thermobifida fusca YX-ER1 at 2.60 A resolution

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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