5cte

From Proteopedia

(Difference between revisions)

Revision as of 12:27, 14 June 2023

Humanized yeast ACC carboxyltransferase domain bound to 2,2-dimethylpropyl (1S)-1-methyl-8-[(7-methyl-1H-indazol-5-yl)carbonyl]-2,8-diazaspiro[4.5]decane-2-carboxylate

Structural highlights

5cte is a 2 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ACAC_YEAST Carries out three functions: biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase. Involved in the synthesis of very-long-chain fatty acid synthesis which is required to maintain a functional nuclear envelope. Required for acylation and vacuolar membrane association of VAC8 which is necessary to maintain a normal morphology of the vacuole.^[1] ^[2] ^[3] ^[4] ^[5]

Publication Abstract from PubMed

A novel series of spirocyclic-diamine based, isoform non-selective inhibitors of acetyl-CoA carboxylase (ACC) is described. These spirodiamine derivatives were discovered by design of a library to mimic the structural rigidity and hydrogen-bonding pattern observed in the co-crystal structure of spirochromanone inhibitor I. The lead compound 3.5.1 inhibited de novo lipogenesis in rat hepatocytes, with an IC50 of 0.30muM.

Discovery of spirocyclic-diamine inhibitors of mammalian acetyl CoA-carboxylase.,Kung DW, Griffith DA, Esler WP, Vajdos FF, Mathiowetz AM, Doran SD, Amor PA, Bagley SW, Banks T, Cabral S, Ford K, Garcia-Irizarry CN, Landis MS, Loomis K, McPherson K, Niosi M, Rockwell KL, Rose C, Smith AC, Southers JA, Tapley S, Tu M, Valentine JJ Bioorg Med Chem Lett. 2015 Sep 15. pii: S0960-894X(15)30067-6. doi:, 10.1016/j.bmcl.2015.09.035. PMID:26411795^[6]

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

References

↑ Mishina M, Roggenkamp R, Schweizer E. Yeast mutants defective in acetyl-coenzyme A carboxylase and biotin: apocarboxylase ligase. Eur J Biochem. 1980 Oct;111(1):79-87. PMID:6108218
↑ Roggenkamp R, Numa S, Schweizer E. Fatty acid-requiring mutant of Saccharomyces cerevisiae defective in acetyl-CoA carboxylase. Proc Natl Acad Sci U S A. 1980 Apr;77(4):1814-7. PMID:6103540
↑ Schneiter R, Hitomi M, Ivessa AS, Fasch EV, Kohlwein SD, Tartakoff AM. A yeast acetyl coenzyme A carboxylase mutant links very-long-chain fatty acid synthesis to the structure and function of the nuclear membrane-pore complex. Mol Cell Biol. 1996 Dec;16(12):7161-72. PMID:8943372
↑ Schneiter R, Guerra CE, Lampl M, Tatzer V, Zellnig G, Klein HL, Kohlwein SD. A novel cold-sensitive allele of the rate-limiting enzyme of fatty acid synthesis, acetyl coenzyme A carboxylase, affects the morphology of the yeast vacuole through acylation of Vac8p. Mol Cell Biol. 2000 May;20(9):2984-95. PMID:10757783
↑ Gao H, Sumanaweera N, Bailer SM, Stochaj U. Nuclear accumulation of the small GTPase Gsp1p depends on nucleoporins Nup133p, Rat2p/Nup120p, Nup85p, Nic96p, and the acetyl-CoA carboxylase Acc1p. J Biol Chem. 2003 Jul 11;278(28):25331-40. Epub 2003 May 1. PMID:12730220 doi:http://dx.doi.org/10.1074/jbc.M301607200
↑ Kung DW, Griffith DA, Esler WP, Vajdos FF, Mathiowetz AM, Doran SD, Amor PA, Bagley SW, Banks T, Cabral S, Ford K, Garcia-Irizarry CN, Landis MS, Loomis K, McPherson K, Niosi M, Rockwell KL, Rose C, Smith AC, Southers JA, Tapley S, Tu M, Valentine JJ. Discovery of spirocyclic-diamine inhibitors of mammalian acetyl CoA-carboxylase. Bioorg Med Chem Lett. 2015 Sep 15. pii: S0960-894X(15)30067-6. doi:, 10.1016/j.bmcl.2015.09.035. PMID:26411795 doi:http://dx.doi.org/10.1016/j.bmcl.2015.09.035

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5cte"

Categories: Large Structures | Saccharomyces cerevisiae | Vajdos FF

@@ Line 1: / Line 1: @@
 ==Humanized yeast ACC carboxyltransferase domain bound to 2,2-dimethylpropyl (1S)-1-methyl-8-[(7-methyl-1H-indazol-5-yl)carbonyl]-2,8-diazaspiro[4.5]decane-2-carboxylate==
-<StructureSection load='5cte' size='340' side='right' caption='[[5cte]], [[Resolution|resolution]] 2.34&Aring;' scene=''>
+<StructureSection load='5cte' size='340' side='right'caption='[[5cte]], [[Resolution|resolution]] 2.34&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5cte]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CTE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CTE FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5cte]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CTE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CTE FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=57L:2,2-DIMETHYLPROPYL+(1S)-1-METHYL-8-[(7-METHYL-1H-INDAZOL-5-YL)CARBONYL]-2,8-DIAZASPIRO[4.5]DECANE-2-CARBOXYLATE'>57L</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=57L:2,2-DIMETHYLPROPYL+(1S)-1-METHYL-8-[(7-METHYL-1H-INDAZOL-5-YL)CARBONYL]-2,8-DIAZASPIRO[4.5]DECANE-2-CARBOXYLATE'>57L</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5ctb|5ctb]], [[5ctc|5ctc]]</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=5cte FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cte OCA], [https://pdbe.org/5cte PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cte RCSB], [https://www.ebi.ac.uk/pdbsum/5cte PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cte ProSAT]</span></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ACC1, ABP2, FAS3, MTR7, YNR016C, N3175 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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=5cte FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cte OCA], [http://pdbe.org/5cte PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5cte RCSB], [http://www.ebi.ac.uk/pdbsum/5cte PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5cte ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/ACAC_YEAST ACAC_YEAST]] Carries out three functions: biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase. Involved in the synthesis of very-long-chain fatty acid synthesis which is required to maintain a functional nuclear envelope. Required for acylation and vacuolar membrane association of VAC8 which is necessary to maintain a normal morphology of the vacuole.<ref>PMID:6108218</ref> <ref>PMID:6103540</ref> <ref>PMID:8943372</ref> <ref>PMID:10757783</ref> <ref>PMID:12730220</ref>
+[https://www.uniprot.org/uniprot/ACAC_YEAST ACAC_YEAST] Carries out three functions: biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase. Involved in the synthesis of very-long-chain fatty acid synthesis which is required to maintain a functional nuclear envelope. Required for acylation and vacuolar membrane association of VAC8 which is necessary to maintain a normal morphology of the vacuole.<ref>PMID:6108218</ref> <ref>PMID:6103540</ref> <ref>PMID:8943372</ref> <ref>PMID:10757783</ref> <ref>PMID:12730220</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 20: / Line 18: @@
 </div>
 <div class="pdbe-citations 5cte" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Acetyl-CoA carboxylase 3D structures|Acetyl-CoA carboxylase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Atcc 18824]]
+[[Category: Large Structures]]
-[[Category: Vajdos, F F]]
+[[Category: Saccharomyces cerevisiae]]
-[[Category: Acc]]
+[[Category: Vajdos FF]]
-[[Category: Inhibitor]]
-[[Category: Transferase-transferase inhibitor complex]]

5cte

From Proteopedia

Revision as of 12:27, 14 June 2023

Humanized yeast ACC carboxyltransferase domain bound to 2,2-dimethylpropyl (1S)-1-methyl-8-[(7-methyl-1H-indazol-5-yl)carbonyl]-2,8-diazaspiro[4.5]decane-2-carboxylate

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox