This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

2ihv

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

Carboxyethylarginine synthase from Streptomyces clavuligerus: 5-guanidinovaleric acid complex

Structural highlights

2ihv is a 4 chain structure with sequence from Streptomyces clavuligerus. 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

CEAS_STRCL Involved in the biosynthesis of the beta-lactamase inhibitor, clavulanic acid. Catalyzes the thiamine diphosphate (ThDP) dependent condensation of D-glyceraldehyde-3-phosphate (D-G3P) with L-arginine to yield the beta-amino acid, N2-(2-carboxyethyl)arginine (CEA) via a beta-elimination resulting in the formation of an enol which undergoes a second elimination to generate the alpha,beta-unsaturated acryloyl-ThDP.^[1] ^[2]

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

N(2)-(2-Carboxyethyl)arginine synthase (CEAS), an unusual thiamin diphosphate (ThDP)-dependent enzyme, catalyses the committed step in the biosynthesis of the b-lactamase inhibitor clavulanic acid in Streptomyces clavuligerus. Crystal structures of tetrameric CEAS-ThDP in complex with the substrate analogues 5-guanidinovaleric acid (GVA) and tartrate, and a structure reflecting a possible enol(ate)-ThDP reaction intermediate are described. The structures suggest overlapping binding sites for the substrates D-glyceraldehyde-3-phosphate (D-G3P) and L-arginine, and are consistent with the proposed CEAS mechanism in which D-G3P binds at the active site and reacts to form an alpha,beta-unsaturated intermediate,which subsequently undergoes (1,4)-Michael addition with the alpha-amino group of L-arginine. Additional solution studies are presented which probe the amino acid substrate tolerance of CEAS, providing further insight into the L-arginine binding site. These findings may facilitate the engineering of CEAS towards the synthesis of alternative beta-amino acid products.

Structural and mechanistic studies on N(2)-(2-carboxyethyl)arginine synthase.,Caines ME, Sorensen JL, Schofield CJ Biochem Biophys Res Commun. 2009 Aug 7;385(4):512-7. Epub 2009 May 27. PMID:19477162^[3]

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

References

↑ Merski M, Townsend CA. Observation of an acryloyl-thiamin diphosphate adduct in the first step of clavulanic acid biosynthesis. J Am Chem Soc. 2007 Dec 26;129(51):15750-1. Epub 2007 Dec 5. PMID:18052280 doi:http://dx.doi.org/10.1021/ja076704r
↑ Caines ME, Sorensen JL, Schofield CJ. Structural and mechanistic studies on N(2)-(2-carboxyethyl)arginine synthase. Biochem Biophys Res Commun. 2009 Aug 7;385(4):512-7. Epub 2009 May 27. PMID:19477162 doi:10.1016/j.bbrc.2009.05.095
↑ Caines ME, Sorensen JL, Schofield CJ. Structural and mechanistic studies on N(2)-(2-carboxyethyl)arginine synthase. Biochem Biophys Res Commun. 2009 Aug 7;385(4):512-7. Epub 2009 May 27. PMID:19477162 doi:10.1016/j.bbrc.2009.05.095

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/2ihv"

Categories: Large Structures | Streptomyces clavuligerus | Caines ME | Schofield CJ

@@ Line 1: / Line 1: @@
 ==Carboxyethylarginine synthase from Streptomyces clavuligerus: 5-guanidinovaleric acid complex==
-<StructureSection load='2ihv' size='340' side='right' caption='[[2ihv]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
+<StructureSection load='2ihv' size='340' side='right'caption='[[2ihv]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2ihv]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/As_4.1611 As 4.1611]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IHV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2IHV FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2ihv]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_clavuligerus Streptomyces clavuligerus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IHV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IHV FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GVA:5-{[AMINO(IMINO)METHYL]AMINO}PENTANOIC+ACID'>GVA</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</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">ceas2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1901 AS 4.1611])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GVA:5-{[AMINO(IMINO)METHYL]AMINO}PENTANOIC+ACID'>GVA</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/N(2)-(2-carboxyethyl)arginine_synthase N(2)-(2-carboxyethyl)arginine synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.66 2.5.1.66] </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=2ihv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ihv OCA], [https://pdbe.org/2ihv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ihv RCSB], [https://www.ebi.ac.uk/pdbsum/2ihv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ihv 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=2ihv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ihv OCA], [http://pdbe.org/2ihv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ihv RCSB], [http://www.ebi.ac.uk/pdbsum/2ihv PDBsum]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/CEAS_STRCL CEAS_STRCL] Involved in the biosynthesis of the beta-lactamase inhibitor, clavulanic acid. Catalyzes the thiamine diphosphate (ThDP) dependent condensation of D-glyceraldehyde-3-phosphate (D-G3P) with L-arginine to yield the beta-amino acid, N2-(2-carboxyethyl)arginine (CEA) via a beta-elimination resulting in the formation of an enol which undergoes a second elimination to generate the alpha,beta-unsaturated acryloyl-ThDP.<ref>PMID:18052280</ref> <ref>PMID:19477162</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/ih/2ihv_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ih/2ihv_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 31: / Line 33: @@
 __TOC__
 </StructureSection>
-[[Category: As 4 1611]]
+[[Category: Large Structures]]
-[[Category: Caines, M E]]
+[[Category: Streptomyces clavuligerus]]
-[[Category: Schofield, C J]]
+[[Category: Caines ME]]
-[[Category: Thiamin diphosphate complex]]
+[[Category: Schofield CJ]]
-[[Category: Transferase]]

2ihv

From Proteopedia

Current revision

Carboxyethylarginine synthase from Streptomyces clavuligerus: 5-guanidinovaleric acid complex

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox