1ot1

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "1ot1" [edit=sysop:move=sysop])
Current revision (09:31, 16 August 2023) (edit) (undo)
 
(8 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1ot1.png|left|200px]]
 
-
{{STRUCTURE_1ot1| PDB=1ot1 | SCENE= }}
+
==Bacillus circulans strain 251 Cyclodextrin glycosyl transferase mutant D135A==
 +
<StructureSection load='1ot1' size='340' side='right'caption='[[1ot1]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1ot1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Niallia_circulans Niallia circulans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OT1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OT1 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]] 2&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=PRD_900001:alpha-maltose'>PRD_900001</scene></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=1ot1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ot1 OCA], [https://pdbe.org/1ot1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ot1 RCSB], [https://www.ebi.ac.uk/pdbsum/1ot1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ot1 ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/CDGT2_NIACI CDGT2_NIACI]
 +
== 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/ot/1ot1_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=1ot1 ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
The alpha-amylase family is a large group of starch processing enzymes [Svensson, B. (1994) Plant Mol. Biol. 25, 141-157]. It is characterized by four short sequence motifs that contain the seven fully conserved amino acid residues in this family: two catalytic carboxylic acid residues and four substrate binding residues. The seventh conserved residue (Asp135) has no direct interactions with either substrates or products, but it is hydrogen-bonded to Arg227, which does bind the substrate in the catalytic site. Using cyclodextrin glycosyltransferase as an example, this paper provides for the first time definite biochemical and structural evidence that Asp135 is required for the proper conformation of several catalytic site residues and therefore for activity.
-
===Bacillus circulans strain 251 Cyclodextrin glycosyl transferase mutant D135A===
+
The fully conserved Asp residue in conserved sequence region I of the alpha-amylase family is crucial for the catalytic site architecture and activity.,Leemhuis H, Rozeboom HJ, Dijkstra BW, Dijkhuizen L FEBS Lett. 2003 Apr 24;541(1-3):47-51. PMID:12706817<ref>PMID:12706817</ref>
-
{{ABSTRACT_PUBMED_12706817}}
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
 
+
</div>
-
==About this Structure==
+
<div class="pdbe-citations 1ot1" style="background-color:#fffaf0;"></div>
-
[[1ot1]] is a 1 chain structure of [[Glycosyltransferase]] with sequence from [http://en.wikipedia.org/wiki/Bacillus_circulans Bacillus circulans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OT1 OCA].
+
==See Also==
==See Also==
-
*[[Glycosyltransferase|Glycosyltransferase]]
+
*[[Glycosyltransferase 3D structures|Glycosyltransferase 3D structures]]
-
 
+
== References ==
-
==Reference==
+
<references/>
-
<ref group="xtra">PMID:012706817</ref><references group="xtra"/>
+
__TOC__
-
[[Category: Bacillus circulans]]
+
</StructureSection>
-
[[Category: Cyclomaltodextrin glucanotransferase]]
+
[[Category: Large Structures]]
-
[[Category: Dijkstra, B W.]]
+
[[Category: Niallia circulans]]
-
[[Category: Rozeboom, H J.]]
+
[[Category: Dijkstra BW]]
-
[[Category: Cyclodextrin]]
+
[[Category: Rozeboom HJ]]
-
[[Category: Glycosyl transferase]]
+
-
[[Category: Transferase]]
+

Current revision

Bacillus circulans strain 251 Cyclodextrin glycosyl transferase mutant D135A

PDB ID 1ot1

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools