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1a98

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XPRTASE FROM E. COLI COMPLEXED WITH GMP

Structural highlights

1a98 is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.25Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

XGPT_ECOLI Acts on guanine, xanthine and to a lesser extent hypoxanthine.^[1]

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

Structures of free, substrate-bound and product-bound forms of Escherichia coli xanthine-guanine phosphoribosyltransferase (XGPRT) have been determined by X-ray crystallography. These are compared with the previously determined structure of magnesium and sulphate-bound XPRT. The structure of free XGPRT at 2.25 A resolution confirms the flexibility of residues in and around a mobile loop identified in other PRTases and shows that the cis-peptide conformation of Arg37 at the active site is maintained in the absence of bound ligands. The structures of XGPRT complexed with the purine base substrates guanine or xanthine in combination with cPRib-PP, an analog of the second substrate PRib-PP, have been solved to 2.0 A resolution. In these two structures the disordered phosphate-binding loop of uncomplexed XGPRT becomes ordered through interactions with the 5'-phosphate group of cPRib-PP. The cyclopentane ring of cPRib-PP has the C3 exo pucker conformation, stabilised by the cPRib-PP-bound Mg2+. The purine base specificity of XGPRT appears to be due to water-mediated interactions between the 2-exocyclic groups of guanine or xanthine and side-chains of Glu136 and Asp140, as well as the main-chain oxygen atom of Ile135. Asp92, together with Lys115, could help stabilise the N7-protonated tautomer of the incoming base and could act as a general base to remove the proton from N7 when the nucleotide product is formed. The 2.6 A resolution structure of XGPRT complexed with product GMP is similar to the substrate-bound complexes. However, the ribose ring of GMP is rotated by approximately 24 degrees compared with the equivalent ring in cPRib-PP. This rotation results in the loss of all interactions between the ribosyl group and the enzyme in the product complex.

Structures of free and complexed forms of Escherichia coli xanthine-guanine phosphoribosyltransferase.,Vos S, Parry RJ, Burns MR, de Jersey J, Martin JL J Mol Biol. 1998 Oct 2;282(4):875-89. PMID:9743633^[2]

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

References

↑ Vos S, de Jersey J, Martin JL. Crystal structure of Escherichia coli xanthine phosphoribosyltransferase. Biochemistry. 1997 Apr 8;36(14):4125-34. PMID:9100006 doi:10.1021/bi962640d
↑ Vos S, Parry RJ, Burns MR, de Jersey J, Martin JL. Structures of free and complexed forms of Escherichia coli xanthine-guanine phosphoribosyltransferase. J Mol Biol. 1998 Oct 2;282(4):875-89. PMID:9743633 doi:10.1006/jmbi.1998.2051

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1a98"

@@ Line 1: / Line 1: @@
 ==XPRTASE FROM E. COLI COMPLEXED WITH GMP==
-<StructureSection load='1a98' size='340' side='right' caption='[[1a98]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
+<StructureSection load='1a98' size='340' side='right'caption='[[1a98]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1a98]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A98 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1A98 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1a98]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A98 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A98 FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GPT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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]] 2.25&#8491;</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Xanthine_phosphoribosyltransferase Xanthine phosphoribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.22 2.4.2.22] </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=1a98 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a98 OCA], [https://pdbe.org/1a98 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a98 RCSB], [https://www.ebi.ac.uk/pdbsum/1a98 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a98 ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1a98 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a98 OCA], [http://pdbe.org/1a98 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1a98 RCSB], [http://www.ebi.ac.uk/pdbsum/1a98 PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/XGPT_ECOLI XGPT_ECOLI]] Acts on guanine, xanthine and to a lesser extent hypoxanthine.<ref>PMID:9100006</ref>
+[https://www.uniprot.org/uniprot/XGPT_ECOLI XGPT_ECOLI] Acts on guanine, xanthine and to a lesser extent hypoxanthine.<ref>PMID:9100006</ref>
 == 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/a9/1a98_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a9/1a98_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 30: / Line 30: @@
 ==See Also==
-*[[Phosphoribosyltransferase|Phosphoribosyltransferase]]
+*[[Phosphoribosyltransferase 3D structures|Phosphoribosyltransferase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Bacillus coli migula 1895]]
+[[Category: Escherichia coli]]
-[[Category: Xanthine phosphoribosyltransferase]]
+[[Category: Large Structures]]
-[[Category: Burns, M R]]
+[[Category: Burns MR]]
-[[Category: Jersey, J De]]
+[[Category: De Jersey J]]
-[[Category: Martin, J L]]
+[[Category: Martin JL]]
-[[Category: Parry, R J]]
+[[Category: Parry RJ]]
-[[Category: Vos, S]]
+[[Category: Vos S]]
-[[Category: Glycosyltransferase]]
-[[Category: Phosphoribosyltransferase]]
-[[Category: Purine salvage enzyme]]
-[[Category: Transferase]]

1a98

From Proteopedia

Current revision

XPRTASE FROM E. COLI COMPLEXED WITH GMP

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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