1ot1: Difference between revisions

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{{Seed}}
[[Image:1ot1.png|left|200px]]


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==Bacillus circulans strain 251 Cyclodextrin glycosyl transferase mutant D135A==
The line below this paragraph, containing "STRUCTURE_1ot1", creates the "Structure Box" on the page.
<StructureSection load='1ot1' size='340' side='right'caption='[[1ot1]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<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>
or leave the SCENE parameter empty for the default display.
</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>
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<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>
{{STRUCTURE_1ot1|  PDB=1ot1  |  SCENE=  }}
<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>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1ot1" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_12706817}}, adds the Publication Abstract to the page
*[[Glycosyltransferase 3D structures|Glycosyltransferase 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 12706817 is the PubMed ID number.
== References ==
-->
<references/>
{{ABSTRACT_PUBMED_12706817}}
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Large Structures]]
1OT1 is a 1 chain 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=1OT1 OCA].
[[Category: Niallia circulans]]
 
[[Category: Dijkstra BW]]
==Reference==
[[Category: Rozeboom HJ]]
<ref group="xtra">PMID:12706817</ref><references group="xtra"/>
[[Category: Bacillus circulans]]
[[Category: Cyclomaltodextrin glucanotransferase]]
[[Category: Dijkstra, B W.]]
[[Category: Rozeboom, H J.]]
[[Category: Cyclodextrin]]
[[Category: Glycosyl transferase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 18:51:37 2009''

Latest revision as of 12:31, 16 August 2023

Bacillus circulans strain 251 Cyclodextrin glycosyl transferase mutant D135ABacillus circulans strain 251 Cyclodextrin glycosyl transferase mutant D135A

Structural highlights

1ot1 is a 1 chain structure with sequence from Niallia circulans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Ligands:, , , , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CDGT2_NIACI

Evolutionary Conservation

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

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.

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Leemhuis H, Rozeboom HJ, Dijkstra BW, Dijkhuizen L. The fully conserved Asp residue in conserved sequence region I of the alpha-amylase family is crucial for the catalytic site architecture and activity. FEBS Lett. 2003 Apr 24;541(1-3):47-51. PMID:12706817

1ot1, resolution 2.00Å

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