5k8g: Difference between revisions

Line 1:

~~'''Unreleased structure'''~~

~~The entry~~ 5k8g is ~~ON HOLD until Paper~~ Publication

==Crystal structure of a putative peptide-binding domain of MpAFP==

== Structural highlights ==

<table><tr><td colspan='2'>[[5k8g]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5K8G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5K8G FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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=5k8g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k8g OCA], [http://pdbe.org/5k8g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5k8g RCSB], [http://www.ebi.ac.uk/pdbsum/5k8g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5k8g ProSAT]</span></td></tr>

</table>

== Publication Abstract from PubMed ==

Bacterial adhesins are modular cell-surface proteins that mediate adherence to other cells, surfaces, and ligands. The Antarctic bacterium Marinomonas primoryensis uses a 1.5-MDa adhesin comprising over 130 domains to position it on ice at the top of the water column for better access to oxygen and nutrients. We have reconstructed this 0.6-mum-long adhesin using a "dissect and build" structural biology approach and have established complementary roles for its five distinct regions. Domains in region I (RI) tether the adhesin to the type I secretion machinery in the periplasm of the bacterium and pass it through the outer membrane. RII comprises ~120 identical immunoglobulin-like beta-sandwich domains that rigidify on binding Ca2+ to project the adhesion regions RIII and RIV into the medium. RIII contains ligand-binding domains that join diatoms and bacteria together in a mixed-species community on the underside of sea ice where incident light is maximal. RIV is the ice-binding domain, and the terminal RV domain contains several "repeats-in-toxin" motifs and a noncleavable signal sequence that target proteins for export via the type I secretion system. Similar structural architecture is present in the adhesins of many pathogenic bacteria and provides a guide to finding and blocking binding domains to weaken infectivity.

~~Authors:~~ Guo, S., Campbell, R., Davies, P.

Structure of a 1.5-MDa adhesin that binds its Antarctic bacterium to diatoms and ice.,Guo S, Stevens CA, Vance TDR, Olijve LLC, Graham LA, Campbell RL, Yazdi SR, Escobedo C, Bar-Dolev M, Yashunsky V, Braslavsky I, Langelaan DN, Smith SP, Allingham JS, Voets IK, Davies PL Sci Adv. 2017 Aug 9;3(8):e1701440. doi: 10.1126/sciadv.1701440. eCollection 2017 , Aug. PMID:28808685<ref>PMID:28808685</ref>

~~Description: Crystal structure~~ of ~~a putative peptide-binding domain~~ of ~~MpAFP~~

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

~~[[Category~~: ~~Unreleased Structures]]~~

</div>

== References ==

__TOC__

</StructureSection>

[[Category: Campbell, R]]

[[Category: Davies, P]]

[[Category: Guo, S]]

[[Category: ~~Davies, P~~]]

[[Category: Antifreeze protein]]

[[Category: Cell adhesion]]

[[Category: Peptide binding]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5k8g is ON HOLD  until Paper Publication
+==Crystal structure of a putative peptide-binding domain of MpAFP==
+<StructureSection load='5k8g' size='340' side='right' caption='[[5k8g]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5k8g]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5K8G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5K8G FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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=5k8g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k8g OCA], [http://pdbe.org/5k8g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5k8g RCSB], [http://www.ebi.ac.uk/pdbsum/5k8g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5k8g ProSAT]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Bacterial adhesins are modular cell-surface proteins that mediate adherence to other cells, surfaces, and ligands. The Antarctic bacterium Marinomonas primoryensis uses a 1.5-MDa adhesin comprising over 130 domains to position it on ice at the top of the water column for better access to oxygen and nutrients. We have reconstructed this 0.6-mum-long adhesin using a "dissect and build" structural biology approach and have established complementary roles for its five distinct regions. Domains in region I (RI) tether the adhesin to the type I secretion machinery in the periplasm of the bacterium and pass it through the outer membrane. RII comprises ~120 identical immunoglobulin-like beta-sandwich domains that rigidify on binding Ca2+ to project the adhesion regions RIII and RIV into the medium. RIII contains ligand-binding domains that join diatoms and bacteria together in a mixed-species community on the underside of sea ice where incident light is maximal. RIV is the ice-binding domain, and the terminal RV domain contains several "repeats-in-toxin" motifs and a noncleavable signal sequence that target proteins for export via the type I secretion system. Similar structural architecture is present in the adhesins of many pathogenic bacteria and provides a guide to finding and blocking binding domains to weaken infectivity.
-Authors: Guo, S., Campbell, R., Davies, P.
+Structure of a 1.5-MDa adhesin that binds its Antarctic bacterium to diatoms and ice.,Guo S, Stevens CA, Vance TDR, Olijve LLC, Graham LA, Campbell RL, Yazdi SR, Escobedo C, Bar-Dolev M, Yashunsky V, Braslavsky I, Langelaan DN, Smith SP, Allingham JS, Voets IK, Davies PL Sci Adv. 2017 Aug 9;3(8):e1701440. doi: 10.1126/sciadv.1701440. eCollection 2017 , Aug. PMID:28808685<ref>PMID:28808685</ref>
-Description: Crystal structure of a putative peptide-binding domain of MpAFP
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 5k8g" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Campbell, R]]
+[[Category: Davies, P]]
 [[Category: Guo, S]]
-[[Category: Davies, P]]
+[[Category: Antifreeze protein]]
+[[Category: Cell adhesion]]
+[[Category: Peptide binding]]