2ben: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:2ben.gif|left|200px]]<br /><applet load="2ben" size="350" color="white" frame="true" align="right" spinBox="true"
-caption="2ben, resolution 1.80&Aring;" />
-'''CRYSTAL STRUCTURE OF THE SERRATIA MARCESCENS CHITIN-BINDING PROTEIN CBP21 Y54A MUTANT.'''<br />
-==Overview==
+==Crystal structure of the Serratia marcescens chitin-binding protein CBP21 Y54A mutant.==
-Chitin proteins are commonly found in bacteria that utilize chitin as a, source of energy. CBP21 is a chitin-binding protein from Serratia, marcescens, a Gram-negative soil bacterium capable of efficient chitin, degradation. When grown on chitin, S. marcescens secretes large amounts of, CBP21, along with chitin-degrading enzymes. In an attempt to understand, the molecular mechanism of CBP21 action, we have determined its crystal, structure at 1.55 angstroms resolution. This is the first structure to be, solved of a family 33 carbohydrate-binding module. The structure reveals a, "budded" fibronectin type III fold consisting of two beta-sheets, arranged, as a beta-sheet sandwich, with a 65-residue "bud" consisting of three, short helices, located between beta-strands 1 and 2. Remarkably, conserved, aromatic residues that have been suggested previously to play a role in, chitin binding were mainly found in the interior of the protein, seemingly, incapable of interacting with chitin, whereas the structure revealed a, surface patch of highly conserved, mainly hydrophilic residues. The roles, of six of these conserved surface-exposed residues (Tyr-54, Glu-55, Glu-60, His-114, Asp-182, and Asn-185) were probed by site-directed, mutagenesis and subsequent binding studies. All single point mutations, lowered the affinity of CBP21 for beta-chitin, as shown by 3-8-fold, increases in the apparent binding constant. Thus, binding of CBP21 to, chitin seems to be mediated primarily by conserved, solvent-exposed, polar, side chains.
+<StructureSection load='2ben' size='340' side='right'caption='[[2ben]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2ben]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Serratia_marcescens Serratia marcescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BEN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BEN 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]] 1.8&#8491;</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=2ben FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ben OCA], [https://pdbe.org/2ben PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ben RCSB], [https://www.ebi.ac.uk/pdbsum/2ben PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ben ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/O83009_SERMA O83009_SERMA]
+== 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/be/2ben_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=2ben ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Chitin proteins are commonly found in bacteria that utilize chitin as a source of energy. CBP21 is a chitin-binding protein from Serratia marcescens, a Gram-negative soil bacterium capable of efficient chitin degradation. When grown on chitin, S. marcescens secretes large amounts of CBP21, along with chitin-degrading enzymes. In an attempt to understand the molecular mechanism of CBP21 action, we have determined its crystal structure at 1.55 angstroms resolution. This is the first structure to be solved of a family 33 carbohydrate-binding module. The structure reveals a "budded" fibronectin type III fold consisting of two beta-sheets, arranged as a beta-sheet sandwich, with a 65-residue "bud" consisting of three short helices, located between beta-strands 1 and 2. Remarkably, conserved aromatic residues that have been suggested previously to play a role in chitin binding were mainly found in the interior of the protein, seemingly incapable of interacting with chitin, whereas the structure revealed a surface patch of highly conserved, mainly hydrophilic residues. The roles of six of these conserved surface-exposed residues (Tyr-54, Glu-55, Glu-60, His-114, Asp-182, and Asn-185) were probed by site-directed mutagenesis and subsequent binding studies. All single point mutations lowered the affinity of CBP21 for beta-chitin, as shown by 3-8-fold increases in the apparent binding constant. Thus, binding of CBP21 to chitin seems to be mediated primarily by conserved, solvent-exposed, polar side chains.
-==About this Structure==
+Crystal structure and binding properties of the Serratia marcescens chitin-binding protein CBP21.,Vaaje-Kolstad G, Houston DR, Riemen AH, Eijsink VG, van Aalten DM J Biol Chem. 2005 Mar 25;280(12):11313-9. Epub 2004 Dec 8. PMID:15590674<ref>PMID:15590674</ref>
-BEN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Serratia_marcescens Serratia marcescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BEN OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-Crystal structure and binding properties of the Serratia marcescens chitin-binding protein CBP21., Vaaje-Kolstad G, Houston DR, Riemen AH, Eijsink VG, van Aalten DM, J Biol Chem. 2005 Mar 25;280(12):11313-9. Epub 2004 Dec 8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15590674 15590674]
+</div>
+<div class="pdbe-citations 2ben" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Serratia marcescens]]
-[[Category: Single protein]]
+[[Category: Eijsink VGH]]
-[[Category: Aalten, D.M.F.Van.]]
+[[Category: Houston DR]]
-[[Category: Eijsink, V.G.H.]]
+[[Category: Vaaje-Kolstad G]]
-[[Category: Houston, D.R.]]
+[[Category: Van Aalten DMF]]
-[[Category: Vaaje-Kolstad, G.]]
-[[Category: chitin degradation]]
-[[Category: chitin-binding]]
-[[Category: fniii-like fold]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 18:22:55 2008''