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6rza

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Revision as of 00:38, 7 March 2020

Cryo-EM structure of the human inner arm dynein DNAH7 microtubule binding domain bound to microtubules

6rza, resolution 5.40Å

Structural highlights

6rza is a 5 chain structure with sequence from Human and Sus scrofa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:	Dync1h1, Dhc1, Dnch1, Dnchc1, Dyhc (HUMAN)
Experimental data:	Check to display Experimental Data
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

[DYHC1_MOUSE] Defects in Dync1h1 are the cause of the 'Legs at odd angles' (LOA) phenotype, an autosomal dominant trait where affected animals display unusual twisting of the body and clenching of the hindlimbs when suspended by the tail. Heterozygotes suffer age-related progressive loss of muscle tone and locomotor ability without major reduction in life-span while homozygotes show a more severe phenotype with an inability to move or feed, and die within 24 hours of birth. LOA mutants display defects in migration of facial motor neuron cell bodies and impaired retrograde transport in spinal cord motor neurons. Defects in Dync1h1 are the cause of the Cramping 1 (Cra1) phenotype, an autosomal dominant trait where affected animals display unusual twisting of the body and clenching of the hindlimbs when suspended by the tail. Heterozygotes suffer age-related progressive loss of muscle tone and locomotor ability without major reduction in life-span while homozygotes show a more severe phenotype with an inability to move or feed, and die within 24 hours of birth.

Function

[DYHC1_MOUSE] Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP. [TBB_PIG] Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain. [TBA1B_PIG] Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain.

Publication Abstract from PubMed

Dyneins are motor proteins responsible for transport in the cytoplasm and the beating of axonemes in cilia and flagella. They bind and release microtubules via a compact microtubule-binding domain (MTBD) at the end of a coiled-coil stalk. We address how cytoplasmic and axonemal dynein MTBDs bind microtubules at near atomic resolution. We decorated microtubules with MTBDs of cytoplasmic dynein-1 and axonemal dynein DNAH7 and determined their cryo-EM structures using helical Relion. The majority of the MTBD is rigid upon binding, with the transition to the high-affinity state controlled by the movement of a single helix at the MTBD interface. DNAH7 contains an 18-residue insertion, found in many axonemal dyneins, that contacts the adjacent protofilament. Unexpectedly, we observe that DNAH7, but not dynein-1, induces large distortions in the microtubule cross-sectional curvature. This raises the possibility that dynein coordination in axonemes is mediated via conformational changes in the microtubule.

Cryo-EM of dynein microtubule-binding domains shows how an axonemal dynein distorts the microtubule.,Lacey SE, He S, Scheres SH, Carter AP Elife. 2019 Jul 2;8. pii: 47145. doi: 10.7554/eLife.47145. PMID:31264960^[1]

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

References

↑ Lacey SE, He S, Scheres SH, Carter AP. Cryo-EM of dynein microtubule-binding domains shows how an axonemal dynein distorts the microtubule. Elife. 2019 Jul 2;8. pii: 47145. doi: 10.7554/eLife.47145. PMID:31264960 doi:http://dx.doi.org/10.7554/eLife.47145

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/6rza"

@@ Line 1: / Line 1: @@
 ==Cryo-EM structure of the human inner arm dynein DNAH7 microtubule binding domain bound to microtubules==
-<StructureSection load='6rza' size='340' side='right'caption='[[6rza]], [[Resolution|resolution]] 5.40&Aring;' scene=''>
+<SX load='6rza' size='340' side='right' viewer='molstar' caption='[[6rza]], [[Resolution|resolution]] 5.40&Aring;' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[6rza]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human] and [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RZA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6RZA FirstGlance]. <br>
@@ Line 24: / Line 24: @@
 <references/>
 __TOC__
-</StructureSection>
+</SX>
 [[Category: Human]]
 [[Category: Large Structures]]

6rza

From Proteopedia

Revision as of 00:38, 7 March 2020

Cryo-EM structure of the human inner arm dynein DNAH7 microtubule binding domain bound to microtubules

Structural highlights

Disease

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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