1ooc

From Proteopedia

(Difference between revisions)

Revision as of 15:07, 27 October 2021

Mutations in the T1.5 loop of pectate lyase A

Structural highlights

1ooc is a 2 chain structure with sequence from "erwinia_carotovora_var._chrysanthemi"_(burkholder_et_al._1953)_dye_1969 "erwinia carotovora var. chrysanthemi" (burkholder et al. 1953) dye 1969. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1jrg, 1jta
Gene:	PELA ("Erwinia carotovora var. chrysanthemi" (Burkholder et al. 1953) Dye 1969)
Activity:	Pectate lyase, with EC number 4.2.2.2
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[PLYA_DICCH] Involved in maceration and soft-rotting of plant tissue.

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

Pectate lyase A (PelA) is a pectate-degrading enzyme secreted by plant pathogens. PelA from Erwinia chrysanthemi has 61% amino-acid identity and a conserved structural similarity to pectate lyase E (PelE). Although similar in structure and sequence, the enzymatic characteristics of PelA differ from those for PelE. A structural alignment of PelA and PelE reveals differences in the T1.5 loop. The sequence of the T1.5 loop in PelA was mutated to the homologous sequence in PelE. The crystal structure of the PelA T1.5 mutant has been solved to 1.6 and 2.9 A resolution. The enzymatic and structural properties of the T1.5 mutant are discussed.

Effect of mutations in the T1.5 loop of pectate lyase A from Erwinia chrysanthemi EC16.,Dehdashti SJ, Doan CN, Chao KL, Yoder MD Acta Crystallogr D Biol Crystallogr. 2003 Jul;59(Pt 7):1339-42. Epub 2003, Jun 27. PMID:12832805^[1]

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

References

↑ Dehdashti SJ, Doan CN, Chao KL, Yoder MD. Effect of mutations in the T1.5 loop of pectate lyase A from Erwinia chrysanthemi EC16. Acta Crystallogr D Biol Crystallogr. 2003 Jul;59(Pt 7):1339-42. Epub 2003, Jun 27. PMID:12832805

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/1ooc"

@@ Line 3: / Line 3: @@
 <StructureSection load='1ooc' size='340' side='right'caption='[[1ooc]], [[Resolution|resolution]] 2.94&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1ooc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"erwinia_carotovora_var._chrysanthemi"_(burkholder_et_al._1953)_dye_1969 "erwinia carotovora var. chrysanthemi" (burkholder et al. 1953) dye 1969]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OOC OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1OOC FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1ooc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"erwinia_carotovora_var._chrysanthemi"_(burkholder_et_al._1953)_dye_1969 "erwinia carotovora var. chrysanthemi" (burkholder et al. 1953) dye 1969]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OOC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OOC FirstGlance]. <br>
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1jrg|1jrg]], [[1jta|1jta]]</div></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PELA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=556 "Erwinia carotovora var. chrysanthemi" (Burkholder et al. 1953) Dye 1969])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PELA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=556 "Erwinia carotovora var. chrysanthemi" (Burkholder et al. 1953) Dye 1969])</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pectate_lyase Pectate lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.2.2 4.2.2.2] </span></td></tr>
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Pectate_lyase Pectate lyase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.2.2 4.2.2.2] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1ooc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ooc OCA], [http://pdbe.org/1ooc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ooc RCSB], [http://www.ebi.ac.uk/pdbsum/1ooc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ooc ProSAT]</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=1ooc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ooc OCA], [https://pdbe.org/1ooc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ooc RCSB], [https://www.ebi.ac.uk/pdbsum/1ooc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ooc ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/PLYA_DICCH PLYA_DICCH]] Involved in maceration and soft-rotting of plant tissue.
+[[https://www.uniprot.org/uniprot/PLYA_DICCH PLYA_DICCH]] Involved in maceration and soft-rotting of plant tissue.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1ooc

From Proteopedia

Revision as of 15:07, 27 October 2021

Mutations in the T1.5 loop of pectate lyase A

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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