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1jgi

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Revision as of 08:53, 17 January 2018

Crystal Structure of the Active Site Mutant Glu328Gln of Amylosucrase from Neisseria polysaccharea in Complex with the Natural Substrate Sucrose

Structural highlights

1jgi is a 1 chain structure with sequence from "neisseria_polysacchareae"_riou_et_al._1983 "neisseria polysacchareae" riou et al. 1983. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1jg9
Activity:	Amylosucrase, with EC number 2.4.1.4
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[AMYS_NEIPO] Catalyzes the synthesis of alpha-glucan from sucrose. Catalyzes, in addition, sucrose hydrolysis, maltose and maltotriose synthesis by successive transfers of the glucosyl moiety of sucrose onto the released glucose, and finally turanose and trehalulose synthesis, these two sucrose isomers being obtained by glucosyl transfer onto fructose.^[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

The structure of amylosucrase from Neisseria polysaccharea in complex with beta-D-glucose has been determined by X-ray crystallography at a resolution of 1.66 A. Additionally, the structure of the inactive active site mutant Glu328Gln in complex with sucrose has been determined to a resolution of 2.0 A. The D-glucose complex shows two well-defined D-glucose molecules, one that binds very strongly in the bottom of a pocket that contains the proposed catalytic residues (at the subsite -1), in a nonstrained (4)C(1) conformation, and one that binds in the packing interface to a symmetry-related molecule. A third weaker D-glucose-binding site is located at the surface near the active site pocket entrance. The orientation of the D-glucose in the active site emphasizes the Glu328 role as the general acid/base. The binary sucrose complex shows one molecule bound in the active site, where the glucosyl moiety is located at the alpha-amylase -1 position and the fructosyl ring occupies subsite +1. Sucrose effectively blocks the only visible access channel to the active site. From analysis of the complex it appears that sucrose binding is primarily obtained through enzyme interactions with the glucosyl ring and that an important part of the enzyme function is a precise alignment of a lone pair of the linking O1 oxygen for hydrogen bond interaction with Glu328. The sucrose specificity appears to be determined primarily by residues Asp144, Asp394, Arg446, and Arg509. Both Asp394 and Arg446 are located in an insert connecting beta-strand 7 and alpha-helix 7 that is much longer in amylosucrase compared to other enzymes from the alpha-amylase family (family 13 of the glycoside hydrolases).

Crystal structures of amylosucrase from Neisseria polysaccharea in complex with D-glucose and the active site mutant Glu328Gln in complex with the natural substrate sucrose.,Mirza O, Skov LK, Remaud-Simeon M, Potocki de Montalk G, Albenne C, Monsan P, Gajhede M Biochemistry. 2001 Jul 31;40(30):9032-9. PMID:11467966^[2]

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

References

↑ De Montalk GP, Remaud-Simeon M, Willemot RM, Planchot V, Monsan P. Sequence analysis of the gene encoding amylosucrase from Neisseria polysaccharea and characterization of the recombinant enzyme. J Bacteriol. 1999 Jan;181(2):375-81. PMID:9882648
↑ Mirza O, Skov LK, Remaud-Simeon M, Potocki de Montalk G, Albenne C, Monsan P, Gajhede M. Crystal structures of amylosucrase from Neisseria polysaccharea in complex with D-glucose and the active site mutant Glu328Gln in complex with the natural substrate sucrose. Biochemistry. 2001 Jul 31;40(30):9032-9. PMID:11467966

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/1jgi"

@@ Line 1: / Line 1: @@
 ==Crystal Structure of the Active Site Mutant Glu328Gln of Amylosucrase from Neisseria polysaccharea in Complex with the Natural Substrate Sucrose==
 <StructureSection load='1jgi' size='340' side='right' caption='[[1jgi]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1jg9|1jg9]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Amylosucrase Amylosucrase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.4 2.4.1.4] </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=1jgi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jgi OCA], [http://pdbe.org/1jgi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jgi RCSB], [http://www.ebi.ac.uk/pdbsum/1jgi PDBsum]</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=1jgi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jgi OCA], [http://pdbe.org/1jgi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jgi RCSB], [http://www.ebi.ac.uk/pdbsum/1jgi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1jgi ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 14: / Line 15: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jg/1jgi_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jg/1jgi_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

1jgi

From Proteopedia

Revision as of 08:53, 17 January 2018

Crystal Structure of the Active Site Mutant Glu328Gln of Amylosucrase from Neisseria polysaccharea in Complex with the Natural Substrate Sucrose

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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