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2pec

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Revision as of 07:10, 29 November 2017

THE REFINED THREE-DIMENSIONAL STRUCTURE OF PECTATE LYASE C FROM ERWINIA CHRYSANTHEMI AT 2.2 ANGSTROMS RESOLUTION: IMPLICATIONS FOR AN ENZYMATIC MECHANISM

Structural highlights

2pec is a 1 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. This structure supersedes the now removed PDB entry 1pec. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	PPEL410 OF PELC ("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

[PLYC_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

A new type of structural domain, composed of all parallel beta strands, has been observed within the last year. An analysis of the basic types suggests that there are two distinct classes: the parallel beta helices, which belong to a tri beta-strand category, and the beta roll, which belongs to a di beta-strand category. The novel structural features of each class are described and the proteins belonging to each category are summarized. Proteins with the parallel beta helix fold include three pectate lyases and the tailspike protein from P22 phage. Proteins with the beta roll fold include two alkaline proteases. Although the parallel beta composition is emphasized, the same set of proteins share another common structural feature with several other proteins containing alpha helices: the polypeptide backbone is folded into a coiled structure in which each coil has the same 3-dimensional arrangement of a group of secondary structural elements. In addition to parallel beta domains, the other groups include the alpha/beta coiled fold, as represented by ribonuclease inhibitor, and the alpha/alpha coiled fold, as represented by lipovitellin and soluble lytic transglycoslyase. Novel features of the alpha/beta and alpha/alpha coiled folds are summarized.

Protein motifs. 3. The parallel beta helix and other coiled folds.,Yoder MD, Jurnak F FASEB J. 1995 Mar;9(5):335-42. PMID:7896002^[1]

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

References

↑ Yoder MD, Jurnak F. Protein motifs. 3. The parallel beta helix and other coiled folds. FASEB J. 1995 Mar;9(5):335-42. PMID:7896002

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/2pec"

Categories: Pectate lyase | Jurnak, F | Yoder, M D

@@ Line 1: / Line 1: @@
 ==THE REFINED THREE-DIMENSIONAL STRUCTURE OF PECTATE LYASE C FROM ERWINIA CHRYSANTHEMI AT 2.2 ANGSTROMS RESOLUTION: IMPLICATIONS FOR AN ENZYMATIC MECHANISM==
 <StructureSection load='2pec' size='340' side='right' caption='[[2pec]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PPEL410 OF PELC ([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='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='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=2pec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pec OCA], [http://pdbe.org/2pec PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2pec RCSB], [http://www.ebi.ac.uk/pdbsum/2pec 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=2pec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pec OCA], [http://pdbe.org/2pec PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2pec RCSB], [http://www.ebi.ac.uk/pdbsum/2pec PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2pec ProSAT]</span></td></tr>
 </table>
 == Function ==

2pec

From Proteopedia

Revision as of 07:10, 29 November 2017

THE REFINED THREE-DIMENSIONAL STRUCTURE OF PECTATE LYASE C FROM ERWINIA CHRYSANTHEMI AT 2.2 ANGSTROMS RESOLUTION: IMPLICATIONS FOR AN ENZYMATIC MECHANISM

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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