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2vbp

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Revision as of 08:39, 12 September 2018

Isopenicillin N synthase with substrate analogue L,L,L-ACAB (unexposed)

Structural highlights

2vbp is a 1 chain structure with sequence from A. nidulans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Related:	1bk0, 1blz, 1hb2, 1hb3, 1hb4, 1obn, 1odm, 1odn, 1qiq, 1qje, 1qjf, 1uzw, 1w03, 1w06, 1w3x, 2bu9, 2ivi, 2ivj, 2vbb, 1hb1, 1ips, 1oc1, 1w04, 1w05, 1w3v, 2bjs, 2jb4, 2vau, 2vbd
Activity:	Isopenicillin-N synthase, with EC number 1.21.3.1
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[IPNS_EMENI] Removes, in the presence of oxygen, 4 hydrogen atoms from delta-L-(alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV) to form the azetidinone and thiazolidine rings of isopenicillin.

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

Isopenicillin N synthase (IPNS) is a non-heme iron(II) oxidase which catalyses the biosynthesis of isopenicillin N (IPN) from the tripeptide delta-l-alpha-aminoadipoyl-l-cysteinyl-d-valine (lld-ACV). Herein we report crystallographic studies to investigate the binding of a truncated lll-substrate in the active site of IPNS. Two epimeric tripeptides have been prepared by solution phase peptide synthesis and crystallised with the enzyme. delta-l-alpha-Aminoadipoyl-l-cysteinyl-d-2-amino-3,3-dideuteriobutyrate (lld-ACd(2)Ab) has the same configuration as the natural substrate lld-ACV at each of its three stereocentres; its epimer delta-l-alpha-aminoadipoyl-l-cysteinyl-l-2-amino-3,3-dideuteriobutyrate (lll-ACd(2)Ab) has the opposite configuration at its third amino acid. lll-ACV has previously been shown to inhibit IPNS turnover of its substrate lld-ACV; the all-protiated tripeptide delta-l-alpha-aminoadipoyl-l-cysteinyl-d-2-aminobutyrate (lld-ACAb) is a substrate for IPNS, being turned over to a mixture of penam and cepham products. Comparisons between the crystal structures of the IPNS:Fe(II):lld-ACd(2)Ab and IPNS:Fe(II):lll-ACd(2)Ab complexes offer a possible rationale for the previously observed inhibitory effects of lll-ACV on IPNS activity.

Crystallographic studies on the binding of selectively deuterated LLD- and LLL-substrate epimers by isopenicillin N synthase.,Ge W, Clifton IJ, Stok JE, Adlington RM, Baldwin JE, Rutledge PJ Biochem Biophys Res Commun. 2010 Aug 6;398(4):659-64. Epub 2010 Jul 13. PMID:20603104^[1]

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

References

↑ Ge W, Clifton IJ, Stok JE, Adlington RM, Baldwin JE, Rutledge PJ. Crystallographic studies on the binding of selectively deuterated LLD- and LLL-substrate epimers by isopenicillin N synthase. Biochem Biophys Res Commun. 2010 Aug 6;398(4):659-64. Epub 2010 Jul 13. PMID:20603104 doi:10.1016/j.bbrc.2010.06.129

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/2vbp"

@@ Line 1: / Line 1: @@
-==ISOPENICILLIN N SYNTHASE WITH SUBSTRATE ANALOGUE L,L,L-ACAB (UNEXPOSED)==
+==Isopenicillin N synthase with substrate analogue L,L,L-ACAB (unexposed)==
 <StructureSection load='2vbp' size='340' side='right' caption='[[2vbp]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
 == Structural highlights ==
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1bk0|1bk0]], [[1blz|1blz]], [[1hb2|1hb2]], [[1hb3|1hb3]], [[1hb4|1hb4]], [[1obn|1obn]], [[1odm|1odm]], [[1odn|1odn]], [[1qiq|1qiq]], [[1qje|1qje]], [[1qjf|1qjf]], [[1uzw|1uzw]], [[1w03|1w03]], [[1w06|1w06]], [[1w3x|1w3x]], [[2bu9|2bu9]], [[2ivi|2ivi]], [[2ivj|2ivj]], [[2vbb|2vbb]], [[1hb1|1hb1]], [[1ips|1ips]], [[1oc1|1oc1]], [[1w04|1w04]], [[1w05|1w05]], [[1w3v|1w3v]], [[2bjs|2bjs]], [[2jb4|2jb4]], [[2vau|2vau]], [[2vbd|2vbd]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Isopenicillin-N_synthase Isopenicillin-N synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.21.3.1 1.21.3.1] </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=2vbp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vbp OCA], [http://pdbe.org/2vbp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vbp RCSB], [http://www.ebi.ac.uk/pdbsum/2vbp 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=2vbp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vbp OCA], [http://pdbe.org/2vbp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vbp RCSB], [http://www.ebi.ac.uk/pdbsum/2vbp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2vbp 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/vb/2vbp_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vb/2vbp_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

2vbp

From Proteopedia

Revision as of 08:39, 12 September 2018

Isopenicillin N synthase with substrate analogue L,L,L-ACAB (unexposed)

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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