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5xam

From Proteopedia

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Current revision

Crystal structure of SecDF in I form at 4 A resolution

Structural highlights

5xam is a 2 chain structure with sequence from Deinococcus radiodurans R1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 4Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q9RTE3_DEIRA Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.[HAMAP-Rule:MF_01464][SAAS:SAAS00541769]

Publication Abstract from PubMed

Protein secretion mediated by SecYEG translocon and SecA ATPase is enhanced by membrane-embedded SecDF by using proton motive force. A previous structural study of SecDF indicated that it comprises 12 transmembrane helices that can conduct protons and three periplasmic domains, which form at least two characterized transition states, termed the F and I forms. We report the structures of full-length SecDF in I form at 2.6- to 2.8-A resolution. The structures revealed that SecDF in I form can generate a tunnel that penetrates the transmembrane region and functions as a proton pathway regulated by a conserved Asp residue of the transmembrane region. In one crystal structure, periplasmic cavity interacts with a molecule, potentially polyethylene glycol, which may mimic a substrate peptide. This study provides structural insights into the Sec protein translocation that allows future analyses to develop a more detailed working model for SecDF.

Tunnel Formation Inferred from the I-Form Structures of the Proton-Driven Protein Secretion Motor SecDF.,Furukawa A, Yoshikaie K, Mori T, Mori H, Morimoto YV, Sugano Y, Iwaki S, Minamino T, Sugita Y, Tanaka Y, Tsukazaki T Cell Rep. 2017 May 2;19(5):895-901. doi: 10.1016/j.celrep.2017.04.030. PMID:28467902^[1]

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

References

↑ Furukawa A, Yoshikaie K, Mori T, Mori H, Morimoto YV, Sugano Y, Iwaki S, Minamino T, Sugita Y, Tanaka Y, Tsukazaki T. Tunnel Formation Inferred from the I-Form Structures of the Proton-Driven Protein Secretion Motor SecDF. Cell Rep. 2017 May 2;19(5):895-901. doi: 10.1016/j.celrep.2017.04.030. PMID:28467902 doi:http://dx.doi.org/10.1016/j.celrep.2017.04.030

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/5xam"

Categories: Deinococcus radiodurans R1 | Large Structures | Furukwa A | Tanaka Y | Tsukazaki T

@@ Line 3: / Line 3: @@
 <StructureSection load='5xam' size='340' side='right'caption='[[5xam]], [[Resolution|resolution]] 4.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5xam]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Deira Deira]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XAM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XAM FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5xam]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Deinococcus_radiodurans_R1 Deinococcus radiodurans R1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XAM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XAM FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3aqp|3aqp]], [[5xan|5xan]], [[5xap|5xap]]</div></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 4&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">secD, secF, DR_1822 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243230 DEIRA])</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=5xam FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xam OCA], [https://pdbe.org/5xam PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xam RCSB], [https://www.ebi.ac.uk/pdbsum/5xam PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xam ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/Q9RTE3_DEIRA Q9RTE3_DEIRA]] Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.[HAMAP-Rule:MF_01464][SAAS:SAAS00541769]
+[https://www.uniprot.org/uniprot/Q9RTE3_DEIRA Q9RTE3_DEIRA] Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.[HAMAP-Rule:MF_01464][SAAS:SAAS00541769]
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 23: / Line 22: @@
 __TOC__
 </StructureSection>
-[[Category: Deira]]
+[[Category: Deinococcus radiodurans R1]]
 [[Category: Large Structures]]
-[[Category: Furukwa, A]]
+[[Category: Furukwa A]]
-[[Category: Tanaka, Y]]
+[[Category: Tanaka Y]]
-[[Category: Tsukazaki, T]]
+[[Category: Tsukazaki T]]
-[[Category: Alfa helical]]
-[[Category: Membrane protein]]
-[[Category: Sec translocon]]

5xam

From Proteopedia

Current revision

Crystal structure of SecDF in I form at 4 A resolution

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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