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2mas

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PURINE NUCLEOSIDE HYDROLASE WITH A TRANSITION STATE INHIBITOR

Structural highlights

2mas is a 4 chain structure with sequence from Crithidia fasciculata. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.3Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

IUNH_CRIFA Catalyzes the hydrolysis of all of the commonly occurring purine and pyrimidine nucleosides into ribose and the associated base, but has a preference for inosine and uridine as substrates.

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

Nucleoside N-ribohydrolases are targets for disruption of purine salvage in the protozoan parasites. The structure of a trypanosomal N-ribohydrolase in complex with a transition-state inhibitor is reported at 2.3 A resolution. The nonspecific nucleoside hydrolase from Crithidia fasciculata cocrystallized with p-aminophenyliminoribitol reveals tightly bound Ca2+ as a catalytic site ligand. The complex with the transition-state inhibitor is characterized by (1) large protein conformational changes to create a hydrophobic leaving group site (2) C3'-exo geometry for the inhibitor, typical of a ribooxocarbenium ion (3) stabilization of the ribooxocarbenium analogue between the neighboring group 5'-hydroxyl and bidentate hydrogen bonds to Asn168; and (4) octacoordinate Ca2+ orients a catalytic site water and is liganded to two hydroxyls of the inhibitor. The mechanism is ribooxocarbenium stabilization with weak leaving group activation and is a departure from glucohydrolases which use paired carboxylates to achieve the transition state.

Trypanosomal nucleoside hydrolase. A novel mechanism from the structure with a transition-state inhibitor.,Degano M, Almo SC, Sacchettini JC, Schramm VL Biochemistry. 1998 May 5;37(18):6277-85. PMID:9572842^[1]

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

References

↑ Degano M, Almo SC, Sacchettini JC, Schramm VL. Trypanosomal nucleoside hydrolase. A novel mechanism from the structure with a transition-state inhibitor. Biochemistry. 1998 May 5;37(18):6277-85. PMID:9572842 doi:http://dx.doi.org/10.1021/bi973012e

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2mas"

Categories: Crithidia fasciculata | Large Structures | Degano M | Sacchettini JC | Schramm VL

@@ Line 3: / Line 3: @@
 <StructureSection load='2mas' size='340' side='right'caption='[[2mas]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2mas]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Crifa Crifa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MAS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MAS FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2mas]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Crithidia_fasciculata Crithidia fasciculata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MAS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MAS FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PIR:2-(4-AMINO-PHENYL)-5-HYDROXYMETHYL-PYRROLIDINE-3,4-DIOL'>PIR</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">IU-NH FROM C. FASCICULATA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5656 CRIFA])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PIR:2-(4-AMINO-PHENYL)-5-HYDROXYMETHYL-PYRROLIDINE-3,4-DIOL'>PIR</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Purine_nucleosidase Purine nucleosidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.1 3.2.2.1] </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=2mas FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mas OCA], [https://pdbe.org/2mas PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mas RCSB], [https://www.ebi.ac.uk/pdbsum/2mas PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mas ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/IUNH_CRIFA IUNH_CRIFA]] Catalyzes the hydrolysis of all of the commonly occurring purine and pyrimidine nucleosides into ribose and the associated base, but has a preference for inosine and uridine as substrates.
+[https://www.uniprot.org/uniprot/IUNH_CRIFA IUNH_CRIFA] Catalyzes the hydrolysis of all of the commonly occurring purine and pyrimidine nucleosides into ribose and the associated base, but has a preference for inosine and uridine as substrates.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 34: / Line 33: @@
 __TOC__
 </StructureSection>
-[[Category: Crifa]]
+[[Category: Crithidia fasciculata]]
 [[Category: Large Structures]]
-[[Category: Purine nucleosidase]]
+[[Category: Degano M]]
-[[Category: Degano, M]]
+[[Category: Sacchettini JC]]
-[[Category: Sacchettini, J C]]
+[[Category: Schramm VL]]
-[[Category: Schramm, V L]]
-[[Category: Hydrolase]]
-[[Category: Inosine]]
-[[Category: Iu-nh]]
-[[Category: Purine nucleoside hydrolase]]
-[[Category: Uridine]]

2mas

From Proteopedia

Current revision

PURINE NUCLEOSIDE HYDROLASE WITH A TRANSITION STATE INHIBITOR

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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