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==The Crystal Structure Analysis of Creatine Amidinohydrolase from Actinobacillus== | |||
<StructureSection load='1kp0' size='340' side='right'caption='[[1kp0]], [[Resolution|resolution]] 2.70Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1kp0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Actinobacillus Actinobacillus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KP0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KP0 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]] 2.7Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLX:GLU/GLN+AMBIGUOUS'>GLX</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=1kp0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kp0 OCA], [https://pdbe.org/1kp0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kp0 RCSB], [https://www.ebi.ac.uk/pdbsum/1kp0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kp0 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q7SIB5_9PAST Q7SIB5_9PAST] | |||
== 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/kp/1kp0_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=1kp0 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The crystal structure of Actinobacillus creatine amidinohydrolase has been solved by molecular replacement. The amino-acid sequence has been derived from the crystal structure. Crystals belong to space group I222, with unit-cell parameters a = 111.26 (3), b = 113.62 (4), c = 191.65 (2) A, and contain two molecules in an asymmetric unit. The structure was refined to an R factor of 18.8% at 2.7 A resolution. The crystal structure contains a dimer of 402 residues and 118 water molecules. The protein structure is bilobal, consisting of a small N-terminal domain and a large C-terminal domain. The C-terminal domain has a pitta-bread fold, similar to that found in Pseudomonas putida creatinase, proline aminopeptidases and methionine aminopeptidase. Comparison with complex crystal structures of P. putida creatinase reveals that the enzyme activity of Actinobacillus creatinase might be similar to that of P. putida creatinase. | |||
Structure of creatine amidinohydrolase from Actinobacillus.,Padmanabhan B, Paehler A, Horikoshi M Acta Crystallogr D Biol Crystallogr. 2002 Aug;58(Pt 8):1322-8. Epub 2002, Jul 20. PMID:12136144<ref>PMID:12136144</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1kp0" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
== | __TOC__ | ||
< | </StructureSection> | ||
[[Category: Actinobacillus]] | [[Category: Actinobacillus]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Horikoshi | [[Category: Horikoshi M]] | ||
[[Category: Padmanabhan | [[Category: Padmanabhan B]] | ||
[[Category: Paehler | [[Category: Paehler A]] | ||
Latest revision as of 10:20, 9 October 2024
The Crystal Structure Analysis of Creatine Amidinohydrolase from ActinobacillusThe Crystal Structure Analysis of Creatine Amidinohydrolase from Actinobacillus
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe crystal structure of Actinobacillus creatine amidinohydrolase has been solved by molecular replacement. The amino-acid sequence has been derived from the crystal structure. Crystals belong to space group I222, with unit-cell parameters a = 111.26 (3), b = 113.62 (4), c = 191.65 (2) A, and contain two molecules in an asymmetric unit. The structure was refined to an R factor of 18.8% at 2.7 A resolution. The crystal structure contains a dimer of 402 residues and 118 water molecules. The protein structure is bilobal, consisting of a small N-terminal domain and a large C-terminal domain. The C-terminal domain has a pitta-bread fold, similar to that found in Pseudomonas putida creatinase, proline aminopeptidases and methionine aminopeptidase. Comparison with complex crystal structures of P. putida creatinase reveals that the enzyme activity of Actinobacillus creatinase might be similar to that of P. putida creatinase. Structure of creatine amidinohydrolase from Actinobacillus.,Padmanabhan B, Paehler A, Horikoshi M Acta Crystallogr D Biol Crystallogr. 2002 Aug;58(Pt 8):1322-8. Epub 2002, Jul 20. PMID:12136144[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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