1e15: Difference between revisions

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==CHITINASE B FROM SERRATIA MARCESCENS==
 
<StructureSection load='1e15' size='340' side='right' caption='[[1e15]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
==Chitinase B from Serratia Marcescens==
<StructureSection load='1e15' size='340' side='right'caption='[[1e15]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1e15]] is a 2 chain structure with 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=1E15 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E15 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1e15]] 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=1E15 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E15 FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ctn|1ctn]]</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]] 1.9&#8491;</td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1e15 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e15 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1e15 RCSB], [http://www.ebi.ac.uk/pdbsum/1e15 PDBsum]</span></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=1e15 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e15 OCA], [https://pdbe.org/1e15 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e15 RCSB], [https://www.ebi.ac.uk/pdbsum/1e15 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e15 ProSAT]</span></td></tr>
<table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q54276_SERMA Q54276_SERMA]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e1/1e15_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e1/1e15_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </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/chain_selection.php?pdb_ID=2ata ConSurf].
</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=1e15 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
In this paper, we describe the structure of chitinase B from Serratia marcescens, which consists of a catalytic domain with a TIM-barrel fold and a 49-residue C-terminal chitin-binding domain. This chitinase is the first structure of a bacterial exochitinase, and it represents one of only a few examples of a glycosyl hydrolase structure having interacting catalytic and substrate-binding domains. The chitin-binding domain has exposed aromatic residues that contribute to a 55-A long continuous aromatic stretch extending into the active site. Binding of chitin oligomers is blocked beyond the -3 subsite, which explains why the enzyme has chitotriosidase activity and degrades the chitin chain from the nonreducing end. Comparison of the chitinase B structure with that of chitinase A explains why these enzymes act synergistically in the degradation of chitin.
Structure of a two-domain chitotriosidase from Serratia marcescens at 1.9-A resolution.,van Aalten DM, Synstad B, Brurberg MB, Hough E, Riise BW, Eijsink VG, Wierenga RK Proc Natl Acad Sci U S A. 2000 May 23;97(11):5842-7. PMID:10823940<ref>PMID:10823940</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>


==See Also==
==See Also==
*[[Chitinase|Chitinase]]
*[[Chitinase 3D structures|Chitinase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Serratia marcescens]]
[[Category: Serratia marcescens]]
[[Category: Aalten, D M.F Van.]]
[[Category: Brurberg MB]]
[[Category: Brurberg, M B.]]
[[Category: Eijsink VGH]]
[[Category: Eijsink, V G.H.]]
[[Category: Hough E]]
[[Category: Hough, E.]]
[[Category: Riise BW]]
[[Category: Riise, B W.]]
[[Category: Synstad B]]
[[Category: Synstad, B.]]
[[Category: Van Aalten DMF]]
[[Category: Wierenga, R K.]]
[[Category: Wierenga RK]]
[[Category: Chitin degradation]]
[[Category: Hydrolase]]

Latest revision as of 12:57, 20 March 2024

Chitinase B from Serratia MarcescensChitinase B from Serratia Marcescens

Structural highlights

1e15 is a 2 chain structure with sequence from Serratia marcescens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q54276_SERMA

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1e15, resolution 1.90Å

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OCA
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