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3s28

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Revision as of 18:52, 1 February 2017

The crystal structure of sucrose synthase-1 in complex with a breakdown product of the UDP-glucose

Structural highlights

3s28 is a 8 chain structure with sequence from Arath. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , , , ,
Related:	3s27, 3s29
Gene:	At5g20830, SUS1, T1M15.230 (ARATH)
Activity:	Sucrose synthase, with EC number 2.4.1.13
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[SUS1_ARATH] Involved in mRNA export coupled transcription activation by association with both the TREX-2 and the SAGA complexes. The transcription regulatory histone acetylation (HAT) complex SAGA is a multiprotein complex that activates transcription by remodeling chromatin and mediating histone acetylation and deubiquitination. Within the SAGA complex, participates in a subcomplex that specifically deubiquitinates histones. The SAGA complex is recruited to specific gene promoters by activators, where it is required for transcription. The TREX-2 complex functions in docking export-competent ribonucleoprotein particles (mRNPs) to the nuclear entrance of the nuclear pore complex (nuclear basket). TREX-2 participates in mRNA export and accurate chromatin positioning in the nucleus by tethering genes to the nuclear periphery (By similarity).

Publication Abstract from PubMed

Sucrose transport is the central system for the allocation of carbon resources in vascular plants. During growth and development, plants control carbon distribution by coordinating sites of sucrose synthesis and cleavage in different plant organs and different cellular locations. Sucrose synthase, which reversibly catalyzes sucrose synthesis and cleavage, provides a direct and reversible means to regulate sucrose flux. Depending on the metabolic environment, sucrose synthase alters its cellular location to participate in cellulose, callose, and starch biosynthesis through its interactions with membranes, organelles, and cytoskeletal actin. The x-ray crystal structure of sucrose synthase isoform 1 from Arabidopsis thaliana (AtSus1) has been determined as a complex with UDP-glucose and as a complex with UDP and fructose, at 2.8- and 2.85-A resolutions, respectively. The AtSus1 structure provides insights into sucrose catalysis and cleavage, as well as the regulation of sucrose synthase and its interactions with cellular targets.

The Structure of Sucrose Synthase-1 from Arabidopsis thaliana and Its Functional Implications.,Zheng Y, Anderson S, Zhang Y, Garavito RM J Biol Chem. 2011 Oct 14;286(41):36108-18. Epub 2011 Aug 24. PMID:21865170^[1]

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

References

↑ Zheng Y, Anderson S, Zhang Y, Garavito RM. The Structure of Sucrose Synthase-1 from Arabidopsis thaliana and Its Functional Implications. J Biol Chem. 2011 Oct 14;286(41):36108-18. Epub 2011 Aug 24. PMID:21865170 doi:10.1074/jbc.M111.275974

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3s28"

@@ Line 1: / Line 1: @@
 ==The crystal structure of sucrose synthase-1 in complex with a breakdown product of the UDP-glucose==
 <StructureSection load='3s28' size='340' side='right' caption='[[3s28]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
@@ Line 7: / Line 8: @@
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">At5g20830, SUS1, T1M15.230 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Sucrose_synthase Sucrose synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.13 2.4.1.13] </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=3s28 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s28 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3s28 RCSB], [http://www.ebi.ac.uk/pdbsum/3s28 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=3s28 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s28 OCA], [http://pdbe.org/3s28 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3s28 RCSB], [http://www.ebi.ac.uk/pdbsum/3s28 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3s28 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 19: / Line 20: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 3s28" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

3s28

From Proteopedia

Revision as of 18:52, 1 February 2017

The crystal structure of sucrose synthase-1 in complex with a breakdown product of the UDP-glucose

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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