Table II.

Proteins with Morphing Regions

		Structures
Name	Disulfide	ox	re	Morphing region	ΔSG Å	Transition Reduced → Oxidized
EcOxyR	199–208	1i6a	1i69	281–298	15.9	Helix, coil to sheet
HsCLIC1	24–59	1rk4	1k0m	27–56	13.5	Sheet to helix, coil
VpChpP	424–493	1v7v	1v7w	483–499	10.8	Strand to coil
SaArsC	82–89	1lju	1jf8	81–95	10.7	Helix to coil
AtCPDase	104–110	1fsi	1jh6	99–119	9.0	C-term of helix to coil
Aebcp	49–54	2cx3	2cx4	44–60	7.6	Helix to β-hairpin
Hs/RnPhe hydroxylase	203–334	1tdw	1phz	131–149	7.2	Helix to coil
HsAKT	60–77	1unr	1unq	39–53	6.8	Helix to coil
SaArsC	10–82	1lk0	1jf8	80–94	5.7	Helix to coil
HsSSAT	120–122	2b5g	2g3t	145–147,155–170	5.2	Coil to strand transition
HsIL2	58–105	1m48	1m4a	29–36, 71–87	5.1	Coil to N-term of helix
TfIMPDH	26–459	1meh	1pvn	317–327,412–435	5.0	Helical phase shift, helix to coil
RnPR-1 Ppase	49–104	1x24	12cl	20–30,46–56,103–110	4.9	R1 helix to coil, R3 coil to helix
EcMurD	208–227	1uag	1eeh	345–354	4.6	Helix to coil transition
HepCRNA polymerase 1a	303–311	1nhu	1c2p	303–318	3.8	β-hairpin straddled by disulfide (motif C) curls in oxidized structure
TtLeu-tRNAs	439–484	1obh	1h3n	150–193, 436–447, 539–546	3.8	Sheet melts, helical phase shift
EcATCase	114–141	1tug	1d09	45–58	3.7	Coil to helix transition
HepCRNA polymerase 2b	316–366	1yvx	1yuy	19–38, 445–451, 539–546	3.6	Helix to coil
HsTSP1	153–214	2es3	1za4	17–29	3.1	Coil to helix transition
MmActivin receptor	86–91	1bte	2goo	58–73, 87–94	3.0	R1 helix to coil, R2 coil to helix
Schem13	193–193a	1txn	1tkl	40–60, 187–202	NA	R1 coil to strand, R2 coil to helix/strand
HsDNA pol III λ	543–543a	1xsl	1xsn	460–474	NA	Strand to coil
HsActivin	80–80a	2arv	2arp	20–27, 65–79	NA	R1 helix to coil transition
						R2 coil to extension of C-term helix
HsRXR	269–269a	1g5y	1fm9	242–264,433–451	NA	Coil to helix R2

Transitions are expressed from reduced to oxidized but are likely to be reversible. Structures where change in SG separation is caused by quaternary structure changes are indicated as NA.

ox, oxidized structure; re, reduced structure; AKT, Rac-alpha serine/threonine kinase; ArsC, arsenate reductase; ATCase, aspartate carbamoyltransferase; bcp, bacterioferritin comigratory protein; ChpP, chitobiose phosphorylase; CLIC1, chloride intracellular channel protein 1; CPDase, cyclic nucleotide phosphodiesterase; DNA pol III λ, DNA polymerase III λ; hem13, coproporphyrinogen III oxidase; IL2, interleukin 2; IMPDH, inosine monophosphate dehydrogenase; Leu-tRNAs, leucyl-tRNA synthetase; MurD, UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase; OxyR, hydrogen peroxide-inducible genes activator; PR-1 Ppase, protein tyrosine phosphatase 4a1; RXR, retinoic acid receptor; SSAT, spermidine/spermine N1-acetyltransferase; TSP1, thrombospondin-1; Ae, Aeropyrum pernix, At, Arabidopsis thaliana; Ec, E. coli; HepC, Hepatitis C; Hs, Homo sapiens; Mm, Mus musculus; Rn, Rattus norvegus; Sa, Staphylococcus aureus; Sc, Saccharomyces cerevisiae; Tf, Tritrichomonas foetus; Tt, Thermus thermophilus; Vp, Vibrio proteolyticus.

^a2nd Cys residue is in another chain (interchain disulfide).