2j71

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (09:35, 9 May 2024) (edit) (undo)
 
(11 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:2j71.jpg|left|200px]]
 
-
{{Structure
+
==alpha-glucan recognition by a family 41 carbohydrate-binding module from Thermotoga maritima pullulanase PulA==
-
|PDB= 2j71 |SIZE=350|CAPTION= <scene name='initialview01'>2j71</scene>, resolution 1.69&Aring;
+
<StructureSection load='2j71' size='340' side='right'caption='[[2j71]], [[Resolution|resolution]] 1.69&Aring;' scene=''>
-
|SITE=
+
== Structural highlights ==
-
|LIGAND=
+
<table><tr><td colspan='2'>[[2j71]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J71 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2J71 FirstGlance]. <br>
-
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Pullulanase Pullulanase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.41 3.2.1.41] </span>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.69&#8491;</td></tr>
-
|GENE=
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2j71 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j71 OCA], [https://pdbe.org/2j71 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2j71 RCSB], [https://www.ebi.ac.uk/pdbsum/2j71 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2j71 ProSAT]</span></td></tr>
-
|DOMAIN=
+
</table>
-
|RELATEDENTRY=
+
== Function ==
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2j71 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j71 OCA], [http://www.ebi.ac.uk/pdbsum/2j71 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2j71 RCSB]</span>
+
[https://www.uniprot.org/uniprot/PULA_THEMA PULA_THEMA]
-
}}
+
== 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/j7/2j71_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=2j71 ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Starch recognition by carbohydrate-binding modules (CBMs) is important for the activity of starch-degrading enzymes. The N-terminal family 41 CBM, TmCBM41 (from pullulanase PulA secreted by Thermotoga maritima) was shown to have alpha-glucan binding activity with specificity for alpha-1,4-glucans but was able to tolerate the alpha-1,6-linkages found roughly every three or four glucose units in pullulan. Using X-ray crystallography, the structures were solved for TmCBM41 in an uncomplexed form and in complex with maltotetraose and 6(3)-alpha-D-glucosyl-maltotriose (GM3). Ligand binding was facilitated by stacking interactions between the alpha-faces of the glucose residues and two tryptophan side-chains in the two main subsites of the carbohydrate-binding site. Overall, this mode of starch binding is quite well conserved by other starch-binding modules. The structure in complex with GM3 revealed a third binding subsite with the flexibility to accommodate an alpha-1,4- or an alpha-1,6-linked glucose.
-
'''ALPHA-GLUCAN RECOGNITION BY A FAMILY 41 CARBOHYDRATE-BINDING MODULE FROM THERMOTOGA MARITIMA PULLULANASE PULA'''
+
The structural basis of alpha-glucan recognition by a family 41 carbohydrate-binding module from Thermotoga maritima.,van Bueren AL, Boraston AB J Mol Biol. 2007 Jan 19;365(3):555-60. Epub 2006 Oct 11. PMID:17095014<ref>PMID:17095014</ref>
-
 
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
==About this Structure==
+
</div>
-
2J71 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J71 OCA].
+
<div class="pdbe-citations 2j71" style="background-color:#fffaf0;"></div>
-
[[Category: Pullulanase]]
+
== References ==
-
[[Category: Single protein]]
+
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Large Structures]]
[[Category: Thermotoga maritima]]
[[Category: Thermotoga maritima]]
-
[[Category: Boraston, A B.]]
+
[[Category: Boraston AB]]
-
[[Category: Bueren, A Lammerts Van.]]
+
[[Category: Lammerts van Bueren A]]
-
[[Category: alpha-glucan binding]]
+
-
[[Category: beta-sandwich fold]]
+
-
[[Category: carbohydrate-binding module]]
+
-
[[Category: glycosidase]]
+
-
[[Category: hydrolase]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:53:55 2008''
+

Current revision

alpha-glucan recognition by a family 41 carbohydrate-binding module from Thermotoga maritima pullulanase PulA

PDB ID 2j71

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2j71"
Personal tools