1ot2: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older edit
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
 
(13 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1ot2.jpg|left|200px]]
<!--
The line below this paragraph, containing "STRUCTURE_1ot2", creates the "Structure Box" on the page.
You may change the PDB parameter (which sets the PDB file loaded into the applet)
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
or leave the SCENE parameter empty for the default display.
-->
{{STRUCTURE_1ot2|  PDB=1ot2  |  SCENE=  }}
'''Bacillus circulans strain 251 Cyclodextrin glycosyl transferase mutant D135N'''


==Bacillus circulans strain 251 Cyclodextrin glycosyl transferase mutant D135N==
<StructureSection load='1ot2' size='340' side='right'caption='[[1ot2]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1ot2]] 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=1OT2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OT2 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]] 2.1&#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=1ot2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ot2 OCA], [https://pdbe.org/1ot2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ot2 RCSB], [https://www.ebi.ac.uk/pdbsum/1ot2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ot2 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/1ot2_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1ot2 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.


==Overview==
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>
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.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1OT2 is a [[Single protein]] structure of 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=1OT2 OCA].
</div>
<div class="pdbe-citations 1ot2" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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:[http://www.ncbi.nlm.nih.gov/pubmed/12706817 12706817]
*[[Glycosyltransferase 3D structures|Glycosyltransferase 3D structures]]
[[Category: Bacillus circulans]]
== References ==
[[Category: Cyclomaltodextrin glucanotransferase]]
<references/>
[[Category: Single protein]]
__TOC__
[[Category: Dijkstra, B W.]]
</StructureSection>
[[Category: Rozeboom, H J.]]
[[Category: Large Structures]]
[[Category: Cyclodextrin]]
[[Category: Niallia circulans]]
[[Category: Glycosyl transferase]]
[[Category: Dijkstra BW]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 04:15:03 2008''
[[Category: Rozeboom HJ]]
Retrieved from "https://proteopedia.org/1ot2"