6sxo

From Proteopedia

(Difference between revisions)

Revision as of 06:36, 19 February 2020

Cryo-EM structure of the human Ebp1-ribosome complex

Structural highlights

6sxo is a 8 chain structure with sequence from [1] and Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

[RL26_HUMAN] Diamond-Blackfan anemia 11 (DBA11) [MIM:614900]: A form of Diamond-Blackfan anemia, a congenital non-regenerative hypoplastic anemia that usually presents early in infancy. Diamond-Blackfan anemia is characterized by a moderate to severe macrocytic anemia, erythroblastopenia, and an increased risk of malignancy. 30 to 40% of Diamond-Blackfan anemia patients present with short stature and congenital anomalies, the most frequent being craniofacial (Pierre-Robin syndrome and cleft palate), thumb and urogenital anomalies. Note=The disease is caused by mutations affecting the gene represented in this entry.^[1]

Function

[PA2G4_HUMAN] May play a role in a ERBB3-regulated signal transduction pathway. Seems be involved in growth regulation. Acts a corepressor of the androgen receptor (AR) and is regulated by the ERBB3 ligand neuregulin-1/heregulin (HRG). Inhibits transcription of some E2F1-regulated promoters, probably by recruiting histone acetylase (HAT) activity. Binds RNA. Associates with 28S, 18S and 5.8S mature rRNAs, several rRNA precursors and probably U3 small nucleolar RNA. May be involved in regulation of intermediate and late steps of rRNA processing. May be involved in ribosome assembly. Mediates cap-independent translation of specific viral IRESs (internal ribosomal entry site) (By similarity).^[2] ^[3] ^[4] ^[5] [RL23A_HUMAN] This protein binds to a specific region on the 26S rRNA (By similarity).

Publication Abstract from PubMed

Human Ebp1 is a member of the proliferation-associated 2G4 (PA2G4) family and plays an important role in cancer regulation. Ebp1 shares the methionine aminopeptidase (MetAP) fold and binds to mature 80S ribosomes for translational control. Here, we present a cryo-EM single particle analysis reconstruction of Ebp1 bound to non-translating human 80S ribosomes at a resolution range from 3.3 to ~8 A. Ebp1 blocks the tunnel exit with major interactions to the general uL23/uL29 docking site for nascent chain-associated factors complemented by eukaryote-specific eL19 and rRNA helix H59. H59 is defined as dynamic adaptor undergoing significant remodeling upon Ebp1 binding. Ebp1 recruits rRNA expansion segment ES27L to the tunnel exit via specific interactions with rRNA consensus sequences. The Ebp1-ribosome complex serves as a template for MetAP binding and provides insights into the structural principles for spatial coordination of co-translational events and molecular triage at the ribosomal tunnel exit.

MetAP-like Ebp1 occupies the human ribosomal tunnel exit and recruits flexible rRNA expansion segments.,Wild K, Aleksic M, Lapouge K, Juaire KD, Flemming D, Pfeffer S, Sinning I Nat Commun. 2020 Feb 7;11(1):776. doi: 10.1038/s41467-020-14603-7. PMID:32034140^[6]

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

References

↑ Gazda HT, Preti M, Sheen MR, O'Donohue MF, Vlachos A, Davies SM, Kattamis A, Doherty L, Landowski M, Buros C, Ghazvinian R, Sieff CA, Newburger PE, Niewiadomska E, Matysiak M, Glader B, Atsidaftos E, Lipton JM, Gleizes PE, Beggs AH. Frameshift mutation in p53 regulator RPL26 is associated with multiple physical abnormalities and a specific pre-ribosomal RNA processing defect in diamond-blackfan anemia. Hum Mutat. 2012 Jul;33(7):1037-44. doi: 10.1002/humu.22081. Epub 2012 Apr 16. PMID:22431104 doi:10.1002/humu.22081
↑ Xia X, Cheng A, Lessor T, Zhang Y, Hamburger AW. Ebp1, an ErbB-3 binding protein, interacts with Rb and affects Rb transcriptional regulation. J Cell Physiol. 2001 May;187(2):209-17. PMID:11268000 doi:http://dx.doi.org/10.1002/jcp.1075
↑ Zhang Y, Woodford N, Xia X, Hamburger AW. Repression of E2F1-mediated transcription by the ErbB3 binding protein Ebp1 involves histone deacetylases. Nucleic Acids Res. 2003 Apr 15;31(8):2168-77. PMID:12682367
↑ Squatrito M, Mancino M, Donzelli M, Areces LB, Draetta GF. EBP1 is a nucleolar growth-regulating protein that is part of pre-ribosomal ribonucleoprotein complexes. Oncogene. 2004 May 27;23(25):4454-65. PMID:15064750 doi:http://dx.doi.org/10.1038/sj.onc.1207579
↑ Zhang Y, Hamburger AW. Specificity and heregulin regulation of Ebp1 (ErbB3 binding protein 1) mediated repression of androgen receptor signalling. Br J Cancer. 2005 Jan 17;92(1):140-6. PMID:15583694 doi:http://dx.doi.org/6602257
↑ Wild K, Aleksic M, Lapouge K, Juaire KD, Flemming D, Pfeffer S, Sinning I. MetAP-like Ebp1 occupies the human ribosomal tunnel exit and recruits flexible rRNA expansion segments. Nat Commun. 2020 Feb 7;11(1):776. doi: 10.1038/s41467-020-14603-7. PMID:32034140 doi:http://dx.doi.org/10.1038/s41467-020-14603-7

1 Structural highlights
2 Disease
3 Function
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/6sxo"

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 6sxo is ON HOLD  until Paper Publication
+==Cryo-EM structure of the human Ebp1-ribosome complex==
+<StructureSection load='6sxo' size='340' side='right'caption='[[6sxo]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6sxo]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SXO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6SXO FirstGlance]. <br>
+</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=6sxo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sxo OCA], [http://pdbe.org/6sxo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6sxo RCSB], [http://www.ebi.ac.uk/pdbsum/6sxo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6sxo ProSAT]</span></td></tr>
+</table>
+== Disease ==
+[[http://www.uniprot.org/uniprot/RL26_HUMAN RL26_HUMAN]] Diamond-Blackfan anemia 11 (DBA11) [MIM:[http://omim.org/entry/614900 614900]]: A form of Diamond-Blackfan anemia, a congenital non-regenerative hypoplastic anemia that usually presents early in infancy. Diamond-Blackfan anemia is characterized by a moderate to severe macrocytic anemia, erythroblastopenia, and an increased risk of malignancy. 30 to 40% of Diamond-Blackfan anemia patients present with short stature and congenital anomalies, the most frequent being craniofacial (Pierre-Robin syndrome and cleft palate), thumb and urogenital anomalies. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:22431104</ref>
+== Function ==
+[[http://www.uniprot.org/uniprot/PA2G4_HUMAN PA2G4_HUMAN]] May play a role in a ERBB3-regulated signal transduction pathway. Seems be involved in growth regulation. Acts a corepressor of the androgen receptor (AR) and is regulated by the ERBB3 ligand neuregulin-1/heregulin (HRG). Inhibits transcription of some E2F1-regulated promoters, probably by recruiting histone acetylase (HAT) activity. Binds RNA. Associates with 28S, 18S and 5.8S mature rRNAs, several rRNA precursors and probably U3 small nucleolar RNA. May be involved in regulation of intermediate and late steps of rRNA processing. May be involved in ribosome assembly. Mediates cap-independent translation of specific viral IRESs (internal ribosomal entry site) (By similarity).<ref>PMID:11268000</ref> <ref>PMID:12682367</ref> <ref>PMID:15064750</ref> <ref>PMID:15583694</ref>  [[http://www.uniprot.org/uniprot/RL23A_HUMAN RL23A_HUMAN]] This protein binds to a specific region on the 26S rRNA (By similarity).
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Human Ebp1 is a member of the proliferation-associated 2G4 (PA2G4) family and plays an important role in cancer regulation. Ebp1 shares the methionine aminopeptidase (MetAP) fold and binds to mature 80S ribosomes for translational control. Here, we present a cryo-EM single particle analysis reconstruction of Ebp1 bound to non-translating human 80S ribosomes at a resolution range from 3.3 to ~8 A. Ebp1 blocks the tunnel exit with major interactions to the general uL23/uL29 docking site for nascent chain-associated factors complemented by eukaryote-specific eL19 and rRNA helix H59. H59 is defined as dynamic adaptor undergoing significant remodeling upon Ebp1 binding. Ebp1 recruits rRNA expansion segment ES27L to the tunnel exit via specific interactions with rRNA consensus sequences. The Ebp1-ribosome complex serves as a template for MetAP binding and provides insights into the structural principles for spatial coordination of co-translational events and molecular triage at the ribosomal tunnel exit.
-Authors:
+MetAP-like Ebp1 occupies the human ribosomal tunnel exit and recruits flexible rRNA expansion segments.,Wild K, Aleksic M, Lapouge K, Juaire KD, Flemming D, Pfeffer S, Sinning I Nat Commun. 2020 Feb 7;11(1):776. doi: 10.1038/s41467-020-14603-7. PMID:32034140<ref>PMID:32034140</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 6sxo" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Aleksic, M]]
+[[Category: Pfeffer, M]]
+[[Category: Sinning, I]]
+[[Category: Wild, K]]
+[[Category: Expansion segment es27l]]
+[[Category: Human ebp1]]
+[[Category: Met-ap homolog]]
+[[Category: Pa2g4 family]]
+[[Category: Ribosome]]

6sxo

From Proteopedia

Revision as of 06:36, 19 February 2020

Cryo-EM structure of the human Ebp1-ribosome complex

Structural highlights

Disease

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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