This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1e15

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (09:57, 20 March 2024) (edit) (undo)
 
Line 3: Line 3:
<StructureSection load='1e15' size='340' side='right'caption='[[1e15]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<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 [https://en.wikipedia.org/wiki/"bacillus_marcescens"_(bizio_1823)_trevisan_in_de_toni_and_trevisan_1889 "bacillus marcescens" (bizio 1823) trevisan in de toni and trevisan 1889]. 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>
+
<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 id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ctn|1ctn]]</div></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 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>
<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]]
Line 17: Line 19:
</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].
</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>
 
-
<div class="pdbe-citations 1e15" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
*[[Chitinase 3D structures|Chitinase 3D structures]]
*[[Chitinase 3D structures|Chitinase 3D structures]]
-
== References ==
 
-
<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Aalten, D M.F Van]]
+
[[Category: Serratia marcescens]]
-
[[Category: Brurberg, M B]]
+
[[Category: Brurberg MB]]
-
[[Category: Eijsink, V G.H]]
+
[[Category: Eijsink VGH]]
-
[[Category: Hough, E]]
+
[[Category: Hough E]]
-
[[Category: Riise, B W]]
+
[[Category: Riise BW]]
-
[[Category: Synstad, B]]
+
[[Category: Synstad B]]
-
[[Category: Wierenga, R K]]
+
[[Category: Van Aalten DMF]]
-
[[Category: Chitin degradation]]
+
[[Category: Wierenga RK]]
-
[[Category: Hydrolase]]
+

Current revision

Chitinase B from Serratia Marcescens

PDB ID 1e15

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools