2wt4: Difference between revisions
No edit summary |
No edit summary |
||
| Line 3: | Line 3: | ||
<StructureSection load='2wt4' size='340' side='right'caption='[[2wt4]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='2wt4' size='340' side='right'caption='[[2wt4]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2wt4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2wt4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WT4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WT4 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ASP:ASPARTIC+ACID'>ASP</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=2wt4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wt4 OCA], [https://pdbe.org/2wt4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wt4 RCSB], [https://www.ebi.ac.uk/pdbsum/2wt4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wt4 ProSAT]</span></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=2wt4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wt4 OCA], [https://pdbe.org/2wt4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wt4 RCSB], [https://www.ebi.ac.uk/pdbsum/2wt4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wt4 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/ASPG_HELPJ ASPG_HELPJ] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 35: | Line 36: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Helicobacter pylori]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Dhavala | [[Category: Dhavala P]] | ||
[[Category: Papageorgiou | [[Category: Papageorgiou AC]] | ||
Latest revision as of 13:16, 9 May 2024
Room temperature crystal structure of Helicobacter pylori L- asparaginase at 1.8 A resolutionRoom temperature crystal structure of Helicobacter pylori L- asparaginase at 1.8 A resolution
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 PubMedBacterial L-asparaginases have been used in the treatment of childhood acute lymphoblastic leukaemia for over 30 years. Their therapeutic effect is based on their ability to catalyze the conversion of L-asparagine, an essential amino acid in certain tumours, to L-aspartic acid and ammonia. Two L-asparaginases, one from Escherichia coli and the other from Erwinia chrysanthemi, have been widely employed in clinical practice as anti-leukaemia drugs. However, L-asparaginases are also able to cause severe side effects owing to their intrinsic glutaminase activity. Helicobacter pylori L-asparaginase (HpA) has been reported to have negligible glutaminase activity. To gain insight into the properties of HpA, its crystal structure in the presence of L-aspartate was determined to 1.4 A resolution, which is one of the highest resolutions obtained for an L-asparaginase structure. The final structure has an R(cryst) of 12.6% (R(free) = 16.9%) with good stereochemistry. A detailed analysis of the active site showed major differences in the active-site flexible loop and in the 286-297 loop from the second subunit, which is involved in active-site formation. Accordingly, Glu289, Asn255 and Gln63 are suggested to play roles in modulating the accessibility of the active site. Overall, the structural comparison revealed that HpA has greater structural similarity to E. coli L-asparaginase than to any other L-asparaginase, including Er. carotovora L-asparaginase, despite the fact that the latter is also characterized by low glutaminase activity. Structure of Helicobacter pylori L-asparaginase at 1.4 A resolution.,Dhavala P, Papageorgiou AC Acta Crystallogr D Biol Crystallogr. 2009 Dec;65(Pt 12):1253-61. Epub 2009, Nov 17. PMID:19966411[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||