8i3j

From Proteopedia

(Difference between revisions)

Revision as of 05:29, 9 August 2023

Crystal structure of human inner-arm dynein heavy chain d stalk and microtubule binding domain

Structural highlights

8i3j is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.69Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

DYH1_HUMAN Non-syndromic male infertility due to sperm motility disorder;Primary ciliary dyskinesia. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry.

Function

DYH1_HUMAN Force generating protein of cilia required for sperm flagellum motility. Produces force towards the minus ends of microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP. Required in spermatozoa for the formation of the inner dynein arms and biogenesis of the axoneme (PubMed:24360805).[UniProtKB:Q91XQ0]^[1]

Publication Abstract from PubMed

Axonemal dynein is an ATP-dependent microtubular motor protein responsible for cilia and flagella beating, and its dysfunction can cause diseases such as primary ciliary dyskinesia and sperm dysmotility. Despite its biological importance, structure-based mechanisms underlying axonemal dynein motors remain unclear. Here, we determined the X-ray crystal structure of the human inner-arm dynein-d (DNAH1) stalk region, which contains a long antiparallel coiled-coil and a microtubule-binding domain (MTBD), at 2.7 A resolution. Notably, differences in the relative orientation of the coiled-coil and MTBD in comparison with other dyneins, as well as the diverse orientations of the MTBD flap region among various isoforms, lead us to propose a 'spike shoe model' with an altered stepping angle for the interaction between IAD-d and microtubules. Based on these findings, we discuss isoform-specific functions of the axonemal dynein stalk MTBDs.

Crystal structure of the stalk region of axonemal inner-arm dynein-d reveals unique features in the coiled-coil and microtubule-binding domain.,Ko S, Toda A, Tanaka H, Yu J, Kurisu G FEBS Lett. 2023 Jul 3. doi: 10.1002/1873-3468.14690. PMID:37400274^[2]

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

References

↑ Ben Khelifa M, Coutton C, Zouari R, Karaouzène T, Rendu J, Bidart M, Yassine S, Pierre V, Delaroche J, Hennebicq S, Grunwald D, Escalier D, Pernet-Gallay K, Jouk PS, Thierry-Mieg N, Touré A, Arnoult C, Ray PF. Mutations in DNAH1, which encodes an inner arm heavy chain dynein, lead to male infertility from multiple morphological abnormalities of the sperm flagella. Am J Hum Genet. 2014 Jan 2;94(1):95-104. PMID:24360805 doi:10.1016/j.ajhg.2013.11.017
↑ Ko S, Toda A, Tanaka H, Yu J, Kurisu G. Crystal structure of the stalk region of axonemal inner-arm dynein-d reveals unique features in the coiled-coil and microtubule-binding domain. FEBS Lett. 2023 Jul 3. PMID:37400274 doi:10.1002/1873-3468.14690

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/8i3j"

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 8i3j is ON HOLD  until Paper Publication
+==Crystal structure of human inner-arm dynein heavy chain d stalk and microtubule binding domain==
+<StructureSection load='8i3j' size='340' side='right'caption='[[8i3j]], [[Resolution|resolution]] 2.69&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[8i3j]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8I3J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8I3J FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.69&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=8i3j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8i3j OCA], [https://pdbe.org/8i3j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8i3j RCSB], [https://www.ebi.ac.uk/pdbsum/8i3j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8i3j ProSAT]</span></td></tr>
+</table>
+== Disease ==
+[https://www.uniprot.org/uniprot/DYH1_HUMAN DYH1_HUMAN] Non-syndromic male infertility due to sperm motility disorder;Primary ciliary dyskinesia. The disease is caused by variants affecting the gene represented in this entry.  The disease is caused by variants affecting the gene represented in this entry.
+== Function ==
+[https://www.uniprot.org/uniprot/DYH1_HUMAN DYH1_HUMAN] Force generating protein of cilia required for sperm flagellum motility. Produces force towards the minus ends of microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP. Required in spermatozoa for the formation of the inner dynein arms and biogenesis of the axoneme (PubMed:24360805).[UniProtKB:Q91XQ0]<ref>PMID:24360805</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Axonemal dynein is an ATP-dependent microtubular motor protein responsible for cilia and flagella beating, and its dysfunction can cause diseases such as primary ciliary dyskinesia and sperm dysmotility. Despite its biological importance, structure-based mechanisms underlying axonemal dynein motors remain unclear. Here, we determined the X-ray crystal structure of the human inner-arm dynein-d (DNAH1) stalk region, which contains a long antiparallel coiled-coil and a microtubule-binding domain (MTBD), at 2.7 A resolution. Notably, differences in the relative orientation of the coiled-coil and MTBD in comparison with other dyneins, as well as the diverse orientations of the MTBD flap region among various isoforms, lead us to propose a 'spike shoe model' with an altered stepping angle for the interaction between IAD-d and microtubules. Based on these findings, we discuss isoform-specific functions of the axonemal dynein stalk MTBDs.
-Authors:
+Crystal structure of the stalk region of axonemal inner-arm dynein-d reveals unique features in the coiled-coil and microtubule-binding domain.,Ko S, Toda A, Tanaka H, Yu J, Kurisu G FEBS Lett. 2023 Jul 3. doi: 10.1002/1873-3468.14690. PMID:37400274<ref>PMID:37400274</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 8i3j" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Ko S]]
+[[Category: Kurisu G]]
+[[Category: Tanaka H]]
+[[Category: Toda A]]
+[[Category: Yu J]]

8i3j

From Proteopedia

Revision as of 05:29, 9 August 2023

Crystal structure of human inner-arm dynein heavy chain d stalk and microtubule binding domain

Structural highlights

Disease

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox